Amino Acids, Proteins, and Enzymes. Primary and Secondary Structure Tertiary and Quaternary Structure Protein Hydrolysis and Denaturation

Save this PDF as:
 WORD  PNG  TXT  JPG

Size: px
Start display at page:

Download "Amino Acids, Proteins, and Enzymes. Primary and Secondary Structure Tertiary and Quaternary Structure Protein Hydrolysis and Denaturation"

Transcription

1 Amino Acids, Proteins, and Enzymes Primary and Secondary Structure Tertiary and Quaternary Structure Protein Hydrolysis and Denaturation 1

2 Primary Structure of Proteins H 3 N The particular sequence of amino acids that is the backbone of a peptide chain or protein CH 3 O+ CH C N H CH 3 CH CH 3 CH CH O C N H SH CH 2 CH O C Ala-Leu-Cys-Met N H CH 3 S CH 2 CH 2 O CH C O - 2

3 Secondary Structure Alpha Helix Three-dimensional arrangement of amino acids with the polypeptide chain in a corkscrew shape Held by H bonds between the H of N-H group and the O of C=O of the fourth amino acid along the chain Looks like a coiled telephone cord 3

4 Secondary Structure Beta Pleated Sheet Polypeptide chains are arranged side by side Hydrogen bonds form between chains R groups of extend above and below the sheet Typical of fibrous proteins such as silk 4

5 Secondary Structure Triple Helix Three polypeptide chains woven together Glycine, proline, hydroxy proline and hydroxylysine H bonding between OH groups gives a strong structure Typical of collagen, connective tissue, skin, tendons, and cartilage 5

6 Learning Check P1 Indicate the type of structure as (1) primary (2) alpha helix (3) beta pleated sheet (4) triple helix A. Polypeptide chain held side by side by H bonds B. Sequence of amino acids in a polypeptide chain C. Corkscrew shape with H bonds between amino acids D. Three peptide chains woven like a rope 6

7 Solution P1 Indicate the type of structure as (1) primary (2) alpha helix (3) beta pleated sheet (4) triple helix A. 3 Polypeptide chain held side by side by H bonds B. 1 Sequence of amino acids in a polypeptide chain C. 2 Corkscrew shape with H bonds between amino acids D. 4 Three peptide chains woven like a rope 7

8 Tertiary Structure Specific overall shape of a protein Cross links between R groups of amino acids in chain disulfide S S + ionic COO H 3 N H bonds C=O HO hydrophobic CH 3 H 3 C 8

9 Learning Check P2 Select the type of tertiary interaction as (1) disulfide (2) ionic (3) H bonds (4) hydrophobic A. Leucine and valine B. Two cysteines C. Aspartic acid and lysine D. Serine and threonine 9

10 Solution P2 Select the type of tertiary interaction as (1) disulfide (2) ionic (3) H bonds (4) hydrophobic A. 4 Leucine and valine B. 1 Two cysteines C. 2 Aspartic acid and lysine D. 3 Serine and threonine 10

11 Globular and Fibrous Proteins Globular proteins spherical shape Insulin Hemoglobin Enzymes Antibodies Fibrous proteins long, thin fibers Hair Wool Skin Nails 11

12 Quaternary Structure Proteins with two or more chains Example is hemoglobin Carries oxygen in blood Four polypeptide chains Each chain has a heme group to bind oxygen 12

13 Learning Check P3 Identify the level of protein structure 1. Primary 2. Secondary 3. Tertiary 4. Quaternary A. Beta pleated sheet B. Order of amino acids in a protein C. A protein with two or more peptide chains D. The shape of a globular protein E. Disulfide bonds between R groups 13

14 Solution P3 Identify the level of protein structure 1. Primary 2. Secondary 3. Tertiary 4. Quaternary A. 2 Beta pleated sheet B. 1 Order of amino acids in a protein C. 4 A protein with two or more peptide chains D. 3 The shape of a globular protein E. 3 Disulfide bonds between R groups 14

15 Protein Hydrolysis Break down of peptide bonds Requires acid or base, water and heat Gives smaller peptides and amino acids Similar to digestion of proteins using enzymes Occurs in cells to provide amino acids to synthesize other proteins and tissues 15

16 Hydrolysis of a Dipeptide + H 3 N CH 3 O CH C + H 3 N N H OH CH 2 CH O C CH 3 O CH COH OH H 2 O, H + heat OH + CH 2 O + H 3 N CH C OH 16

17 Denaturation Disruption of secondary, tertiary and quaternary protein structure by heat/organics Break apart H bonds and disrupt hydrophobic attractions acids/ bases Break H bonds between polar R groups and ionic bonds heavy metal ions React with S-S bonds to form solids agitation 17 Stretches chains until bonds break

18 Applications of Denaturation Hard boiling an egg Wiping the skin with alcohol swab for injection Cooking food to destroy E. coli. Heat used to cauterize blood vessels Autoclave sterilizes instruments Milk is heated to make yogurt 18

19 Learning Check P4 What are the products of the complete hydrolysis of Ala-Ser-Val? 19

20 Solution P4 The products of the complete hydrolysis of Ala-Ser-Val are alanine serine valine 20

21 Learning Check P5 Tannic acid is used to form a scab on a burn. An egg becomes hard boiled when placed in hot water. What is similar about these two events? 21

22 Solution P5 Acid and heat cause a denaturation of protein. They both break bonds in the secondary and tertiary structure of protein. 22

Chapter 19 Amino Acids and Proteins

Chapter 19 Amino Acids and Proteins Chapter 19 Amino Acids and Proteins 19.1 Proteins and Amino Acids 19.2 Amino Acids as Acids and Bases Copyright 2007 by Pearson Education, Inc. Publishing as Benjamin Cummings 1 Functions of Proteins Proteins

More information

Chapter 16 Amino Acids, Proteins, and Enzymes. Functions of Proteins. Examples of Amino Acids. Amino Acids. Nonpolar Amino Acids. Types of Amino Acids

Chapter 16 Amino Acids, Proteins, and Enzymes. Functions of Proteins. Examples of Amino Acids. Amino Acids. Nonpolar Amino Acids. Types of Amino Acids Chapter 16 Amino Acids, Proteins, and Enzymes 16.1 Functions of Proteins 16.2 Amino Acids 16.3 Amino Acids as Acids and Bases Functions of Proteins Proteins perform many different functions in the body.

More information

Chapter 16 Amino Acids, Proteins, and Enzymes

Chapter 16 Amino Acids, Proteins, and Enzymes Chapter 16 Amino Acids, Proteins, and Enzymes 1 Functions of Proteins Proteins in the body are polymers made from 20 different amino acids differ in characteristics and functions that depend on the order

More information

Built from 20 kinds of amino acids

Built from 20 kinds of amino acids Built from 20 kinds of amino acids Each Protein has a three dimensional structure. Majority of proteins are compact. Highly convoluted molecules. Proteins are folded polypeptides. There are four levels

More information

Pipe Cleaner Proteins. Essential question: How does the structure of proteins relate to their function in the cell?

Pipe Cleaner Proteins. Essential question: How does the structure of proteins relate to their function in the cell? Pipe Cleaner Proteins GPS: SB1 Students will analyze the nature of the relationships between structures and functions in living cells. Essential question: How does the structure of proteins relate to their

More information

18.2 Protein Structure and Function: An Overview

18.2 Protein Structure and Function: An Overview 18.2 Protein Structure and Function: An Overview Protein: A large biological molecule made of many amino acids linked together through peptide bonds. Alpha-amino acid: Compound with an amino group bonded

More information

http://faculty.sau.edu.sa/h.alshehri

http://faculty.sau.edu.sa/h.alshehri http://faculty.sau.edu.sa/h.alshehri Definition: Proteins are macromolecules with a backbone formed by polymerization of amino acids. Proteins carry out a number of functions in living organisms: - They

More information

Exam 4 Outline CH 105 Spring 2012

Exam 4 Outline CH 105 Spring 2012 Exam 4 Outline CH 105 Spring 2012 You need to bring a pencil and your ACT card. Chapter 24: Lipids 1. Describe the properties and types of lipids a. All are hydrophobic b. Fatty acid-based typically contain

More information

Structure of proteins

Structure of proteins Structure of proteins Primary structure: is amino acids sequence or the covalent structure (50-2500) amino acids M.Wt. of amino acid=110 Dalton (56 110=5610 Dalton). Single chain or more than one polypeptide

More information

Amino Acids and Proteins

Amino Acids and Proteins Amino Acids and Proteins Proteins are composed of amino acids. There are 20 amino acids commonly found in proteins. All have: N2 C α R COO Amino acids at neutral p are dipolar ions (zwitterions) because

More information

IV. -Amino Acids: carboxyl and amino groups bonded to -Carbon. V. Polypeptides and Proteins

IV. -Amino Acids: carboxyl and amino groups bonded to -Carbon. V. Polypeptides and Proteins IV. -Amino Acids: carboxyl and amino groups bonded to -Carbon A. Acid/Base properties 1. carboxyl group is proton donor! weak acid 2. amino group is proton acceptor! weak base 3. At physiological ph: H

More information

Biological Molecules

Biological Molecules Biological Molecules I won t lie. This is probably the most boring topic you have ever done in any science. It s pretty much as simple as this: learn the material deal with it. Enjoy don t say I didn t

More information

Chapter 12 - Proteins

Chapter 12 - Proteins Roles of Biomolecules Carbohydrates Lipids Proteins 1) Catalytic 2) Transport 3) Regulatory 4) Structural 5) Contractile 6) Protective 7) Storage Nucleic Acids 12.1 -Amino Acids Chapter 12 - Proteins Amino

More information

Advanced Medicinal & Pharmaceutical Chemistry CHEM 5412 Dept. of Chemistry, TAMUK

Advanced Medicinal & Pharmaceutical Chemistry CHEM 5412 Dept. of Chemistry, TAMUK Advanced Medicinal & Pharmaceutical Chemistry CHEM 5412 Dept. of Chemistry, TAMUK Dai Lu, Ph.D. dlu@tamhsc.edu Tel: 361-221-0745 Office: RCOP, Room 307 Drug Discovery and Development Drug Molecules Medicinal

More information

Recap. Lecture 2. Protein conformation. Proteins. 8 types of protein function 10/21/10. Proteins.. > 50% dry weight of a cell

Recap. Lecture 2. Protein conformation. Proteins. 8 types of protein function 10/21/10. Proteins.. > 50% dry weight of a cell Lecture 2 Protein conformation ecap Proteins.. > 50% dry weight of a cell ell s building blocks and molecular tools. More important than genes A large variety of functions http://www.tcd.ie/biochemistry/courses/jf_lectures.php

More information

Part A: Amino Acids and Peptides (Is the peptide IAG the same as the peptide GAI?)

Part A: Amino Acids and Peptides (Is the peptide IAG the same as the peptide GAI?) ChemActivity 46 Amino Acids, Polypeptides and Proteins 1 ChemActivity 46 Part A: Amino Acids and Peptides (Is the peptide IAG the same as the peptide GAI?) Model 1: The 20 Amino Acids at Biological p See

More information

Helices From Readily in Biological Structures

Helices From Readily in Biological Structures The α Helix and the β Sheet Are Common Folding Patterns Although the overall conformation each protein is unique, there are only two different folding patterns are present in all proteins, which are α

More information

The Organic Chemistry of Amino Acids, Peptides, and Proteins

The Organic Chemistry of Amino Acids, Peptides, and Proteins Essential rganic Chemistry Chapter 16 The rganic Chemistry of Amino Acids, Peptides, and Proteins Amino Acids a-amino carboxylic acids. The building blocks from which proteins are made. H 2 N C 2 H Note:

More information

Carbohydrates, proteins and lipids

Carbohydrates, proteins and lipids Carbohydrates, proteins and lipids Chapter 3 MACROMOLECULES Macromolecules: polymers with molecular weights >1,000 Functional groups THE FOUR MACROMOLECULES IN LIFE Molecules in living organisms: proteins,

More information

Concept 5.4: Proteins include a diversity of structures, resulting in a wide range of functions

Concept 5.4: Proteins include a diversity of structures, resulting in a wide range of functions Concept 5.4: Proteins include a diversity of structures, resulting in a wide range of functions Proteins account for more than 50% of the dry mass of most cells Some proteins speed up chemical reactions

More information

Paper: 6 Chemistry 2.130 University I Chemistry: Models Page: 2 of 7. 4. Which of the following weak acids would make the best buffer at ph = 5.0?

Paper: 6 Chemistry 2.130 University I Chemistry: Models Page: 2 of 7. 4. Which of the following weak acids would make the best buffer at ph = 5.0? Paper: 6 Chemistry 2.130 University I Chemistry: Models Page: 2 of 7 4. Which of the following weak acids would make the best buffer at ph = 5.0? A) Acetic acid (Ka = 1.74 x 10-5 ) B) H 2 PO - 4 (Ka =

More information

Ch18_PT MULTIPLE CHOICE. Choose the one alternative that best completes the statement or answers the question.

Ch18_PT MULTIPLE CHOICE. Choose the one alternative that best completes the statement or answers the question. Ch18_PT MULTIPLE CHOICE. Choose the one alternative that best completes the statement or answers the question. 1) All of the following can be classified as biomolecules except A) lipids. B) proteins. C)

More information

I N V E S T I C E D O R O Z V O J E V Z D Ě L Á V Á N Í

I N V E S T I C E D O R O Z V O J E V Z D Ě L Á V Á N Í I V E S T I E D Z V J E V Z D Ě L Á V Á Í AMIAIDS PEPTIDES AMIAIDS = substitutional/functional derivatives of carboxylic acids = basic units of proteins (2-aminoacids) General formula of 2-aminoacids (α-aminoacids):

More information

8/20/2012 H C OH H R. Proteins

8/20/2012 H C OH H R. Proteins Proteins Rubisco monomer = amino acids 20 different amino acids polymer = polypeptide protein can be one or more polypeptide chains folded & bonded together large & complex 3-D shape hemoglobin Amino acids

More information

1. 1. Amino acids and proteins. 1: Biochemistry of macromolecules and metabolic pathways. Key terms

1. 1. Amino acids and proteins. 1: Biochemistry of macromolecules and metabolic pathways. Key terms 1. 1 Amino acids and proteins Key terms Polymer: A large molecule made from repeating units called monomers. Monomer: A molecule that is a basic unit; many monomers join together to make a polymer. Amino

More information

Molecules of Life. Chapter 3 Part 2

Molecules of Life. Chapter 3 Part 2 Molecules of Life Chapter 3 Part 2 3.5 Proteins Diversity in Structure and Function Proteins are the most diverse biological molecule (structural, nutritious, enzyme, transport, communication, and defense

More information

Amino Acids, Peptides, Proteins

Amino Acids, Peptides, Proteins Amino Acids, Peptides, Proteins Functions of proteins: Enzymes Transport and Storage Motion, muscle contraction Hormones Mechanical support Immune protection (Antibodies) Generate and transmit nerve impulses

More information

CHAPTER 29 AMINO ACIDS, POLYPEPTIDES, AND PROTEINS SOLUTIONS TO REVIEW QUESTIONS

CHAPTER 29 AMINO ACIDS, POLYPEPTIDES, AND PROTEINS SOLUTIONS TO REVIEW QUESTIONS APTER 29 AMI AIDS, PLYPEPTIDES, AD PRTEIS SLUTIS T REVIEW QUESTIS 1. The designation, α, means that the amine group in common amino acids is connected to the carbon immediately adjacent to the carboxylic

More information

A. A peptide with 12 amino acids has the following amino acid composition: 2 Met, 1 Tyr, 1 Trp, 2 Glu, 1 Lys, 1 Arg, 1 Thr, 1 Asn, 1 Ile, 1 Cys

A. A peptide with 12 amino acids has the following amino acid composition: 2 Met, 1 Tyr, 1 Trp, 2 Glu, 1 Lys, 1 Arg, 1 Thr, 1 Asn, 1 Ile, 1 Cys Questions- Proteins & Enzymes A. A peptide with 12 amino acids has the following amino acid composition: 2 Met, 1 Tyr, 1 Trp, 2 Glu, 1 Lys, 1 Arg, 1 Thr, 1 Asn, 1 Ile, 1 Cys Reaction of the intact peptide

More information

Proteins. Proteins. Amino Acids. Most diverse and most important molecule in. Functions: Functions (cont d)

Proteins. Proteins. Amino Acids. Most diverse and most important molecule in. Functions: Functions (cont d) Proteins Proteins Most diverse and most important molecule in living i organisms Functions: 1. Structural (keratin in hair, collagen in ligaments) 2. Storage (casein in mother s milk) 3. Transport (HAEMOGLOBIN!)

More information

Structure and properties of proteins. Vladimíra Kvasnicová

Structure and properties of proteins. Vladimíra Kvasnicová Structure and properties of proteins Vladimíra Kvasnicová Chemical nature of proteins biopolymers of amino acids macromolecules (M r > 10 000) Classification of proteins 1) by localization in an organism

More information

Smaller coiled-coil structures are also found at the interaction interface between. Copyright Mark Brandt, Ph.D. 42

Smaller coiled-coil structures are also found at the interaction interface between. Copyright Mark Brandt, Ph.D. 42 Examples of tein Structures tein types teins fall into three general classes, based on their overall three-dimensional structure and on their functional role: fibrous, membrane, and globular. Fibrous proteins

More information

the nature and importance of biomacromolecules in the chemistry of the cell: synthesis of biomacromolecules through the condensation reaction lipids

the nature and importance of biomacromolecules in the chemistry of the cell: synthesis of biomacromolecules through the condensation reaction lipids the nature and importance of biomacromolecules in the chemistry of the cell: synthesis of biomacromolecules through the condensation reaction lipids and their sub-units; the role of lipids in the plasma

More information

INTRODUCTION TO PROTEIN STRUCTURE

INTRODUCTION TO PROTEIN STRUCTURE Name Class: Partner, if any: INTRODUCTION TO PROTEIN STRUCTURE PRIMARY STRUCTURE: 1. Write the complete structural formula of the tripeptide shown (frame 10). Circle and label the three sidechains which

More information

The amino acids differ in the properties of their side chains. Hydrophobic, non acidic (the H+ ion won t associate with water)

The amino acids differ in the properties of their side chains. Hydrophobic, non acidic (the H+ ion won t associate with water) Amino Acids 101 What is an amino acid? Amino acids, or alpha- amino acids, are the building blocks of peptides and proteins They are composed of amine and carboxylic acid groups, separated by the alpha-carbon

More information

Disulfide Bonds at the Hair Salon

Disulfide Bonds at the Hair Salon Disulfide Bonds at the Hair Salon Three Alpha Helices Stabilized By Disulfide Bonds! In order for hair to grow 6 inches in one year, 9 1/2 turns of α helix must be produced every second!!! In some proteins,

More information

Shu-Ping Lin, Ph.D. E-mail: splin@dragon.nchu.edu.tw

Shu-Ping Lin, Ph.D. E-mail: splin@dragon.nchu.edu.tw Amino Acids & Proteins Shu-Ping Lin, Ph.D. Institute te of Biomedical Engineering ing E-mail: splin@dragon.nchu.edu.tw Website: http://web.nchu.edu.tw/pweb/users/splin/ edu tw/pweb/users/splin/ Date: 10.13.2010

More information

Chapter 5. The Structure and Function of Macromolecule s

Chapter 5. The Structure and Function of Macromolecule s Chapter 5 The Structure and Function of Macromolecule s Most Macromolecules are polymers: Polymer: (poly: many; mer: part) Large molecules consisting of many identical or similar subunits connected together.

More information

Chemistry: Introduction to General, Organic & Biological Chemistry (Timberlake) Chapter 16: Amino Acids, Proteins, and Enzymes

Chemistry: Introduction to General, Organic & Biological Chemistry (Timberlake) Chapter 16: Amino Acids, Proteins, and Enzymes Chemistry: Introduction to General, Organic & Biological Chemistry (Timberlake) Chapter 16: Amino Acids, Proteins, and Enzymes MULTIPLE CHOICE 1) Which of the following is NOT a function of proteins? A)

More information

Solution key Problem Set 1

Solution key Problem Set 1 Solution key-7.016 Problem Set 1 Question 1 The following line-angle drawings represent three chemical structures. On each drawing, the hydrogen atoms that should be bonded to the NON-carbon atoms are

More information

Lecture 13-14 Conformation of proteins Conformation of a protein three-dimensional structure native state. native condition

Lecture 13-14 Conformation of proteins Conformation of a protein  three-dimensional structure native state. native condition Lecture 13-14 Conformation of proteins Conformation of a protein refers to the three-dimensional structure in its native state. There are many different possible conformations for a molecule as large as

More information

A disaccharide is formed when a dehydration reaction joins two monosaccharides. This covalent bond is called a glycosidic linkage.

A disaccharide is formed when a dehydration reaction joins two monosaccharides. This covalent bond is called a glycosidic linkage. CH 5 Structure & Function of Large Molecules: Macromolecules Molecules of Life All living things are made up of four classes of large biological molecules: carbohydrates, lipids, proteins, and nucleic

More information

Chapter 3 Molecules of Cells

Chapter 3 Molecules of Cells Bio 100 Molecules of cells 1 Chapter 3 Molecules of Cells Compounds containing carbon are called organic compounds Molecules such as methane that are only composed of carbon and hydrogen are called hydrocarbons

More information

Disaccharides consist of two monosaccharide monomers covalently linked by a glycosidic bond. They function in sugar transport.

Disaccharides consist of two monosaccharide monomers covalently linked by a glycosidic bond. They function in sugar transport. 1. The fundamental life processes of plants and animals depend on a variety of chemical reactions that occur in specialized areas of the organism s cells. As a basis for understanding this concept: 1.

More information

Lecture 1. Introduction

Lecture 1. Introduction Lecture 1 Introduction Before coming to class consider the analogy of the cell as being the city. Where in a city are the plans and all of the directions to run and maintain the city come from? What would

More information

Chemistry 110. Bettelheim, Brown, Campbell & Farrell. Introduction to General, Organic and Biochemistry Chapter 22 Proteins

Chemistry 110. Bettelheim, Brown, Campbell & Farrell. Introduction to General, Organic and Biochemistry Chapter 22 Proteins hemistry 110 Bettelheim, Brown, ampbell & Farrell Ninth Edition Introduction to General, rganic and Biochemistry hapter 22 Proteins Step-growth polyamide (polypeptide) polymers or oligomers of L-α-aminoacids.

More information

I. Polymers & Macromolecules Figure 1: Polymers. Polymer: Macromolecule: Figure 2: Dehydration Synthesis

I. Polymers & Macromolecules Figure 1: Polymers. Polymer: Macromolecule: Figure 2: Dehydration Synthesis I. Polymers & Macromolecules Figure 1: Polymers Polymer: Macromolecule: Figure 2: Dehydration Synthesis 1 Dehydration Synthesis: Figure 3: Hydrolysis Hydrolysis: II. Organic Macromolecules Class I: Carbohydrates:

More information

MCAT Organic Chemistry - Problem Drill 23: Amino Acids, Peptides and Proteins

MCAT Organic Chemistry - Problem Drill 23: Amino Acids, Peptides and Proteins MCAT rganic Chemistry - Problem Drill 23: Amino Acids, Peptides and Proteins Question No. 1 of 10 Question 1. Which amino acid does not contain a chiral center? Question #01 (A) Serine (B) Proline (C)

More information

Conformational Properties of Polypeptide Chains

Conformational Properties of Polypeptide Chains Conformational Properties of Polypeptide Chains Levels of Organization Primary structure Amino acid sequence of the protein Secondary structure H bonds in the peptide chain backbone α helix and β sheets

More information

Worksheet 13.1. Chapter 13: Human biochemistry glossary

Worksheet 13.1. Chapter 13: Human biochemistry glossary Worksheet 13.1 Chapter 13: Human biochemistry glossary α-helix Refers to a secondary structure of a protein where the chain is twisted to form a regular helix, held by hydrogen bonds between peptide bonds

More information

Peptide Bond Amino acids are linked together by peptide bonds to form polypepetide chain.

Peptide Bond Amino acids are linked together by peptide bonds to form polypepetide chain. Peptide Bond Peptide Bond Amino acids are linked together by peptide bonds to form polypepetide chain. + H 2 O 2 Peptide bonds are strong and not broken by conditions that denature proteins, such as heating.

More information

At physiological PH (7.4), -COOH gp is dissociated forming a negatively charged carboxylate ion (COO - ) and amino gp is protonated forming

At physiological PH (7.4), -COOH gp is dissociated forming a negatively charged carboxylate ion (COO - ) and amino gp is protonated forming Amino Acids Amino Acids are the building units of proteins. Proteins are polymers of amino acids linked together by what is called Peptide bond (illustrated below). There are about 300 amino acids occur

More information

Proteins the primary biological macromolecules of living organisms

Proteins the primary biological macromolecules of living organisms Proteins the primary biological macromolecules of living organisms Protein structure and folding Primary Secondary Tertiary Quaternary structure of proteins Structure of Proteins Protein molecules adopt

More information

Structures of Proteins. Primary structure - amino acid sequence

Structures of Proteins. Primary structure - amino acid sequence Structures of Proteins Primary structure - amino acid sequence Secondary structure chain of covalently linked amino acids folds into regularly repeating structures. Secondary structure is the result of

More information

Nafith Abu Tarboush DDS, MSc, PhD natarboush@ju.edu.jo www.facebook.com/natarboush

Nafith Abu Tarboush DDS, MSc, PhD natarboush@ju.edu.jo www.facebook.com/natarboush Nafith Abu Tarboush DDS, MSc, PhD natarboush@ju.edu.jo www.facebook.com/natarboush α-keratins, bundles of α- helices Contain polypeptide chains organized approximately parallel along a single axis: Consist

More information

Proteins and Nucleic Acids

Proteins and Nucleic Acids Proteins and Nucleic Acids Chapter 5 Macromolecules: Proteins Proteins Most structurally & functionally diverse group of biomolecules. : o Involved in almost everything o Enzymes o Structure (keratin,

More information

Protein Physics. A. V. Finkelstein & O. B. Ptitsyn LECTURE 1

Protein Physics. A. V. Finkelstein & O. B. Ptitsyn LECTURE 1 Protein Physics A. V. Finkelstein & O. B. Ptitsyn LECTURE 1 PROTEINS Functions in a Cell MOLECULAR MACHINES BUILDING BLOCKS of a CELL ARMS of a CELL ENZYMES - enzymatic catalysis of biochemical reactions

More information

Biochemistry - I. Prof. S. Dasgupta Department of Chemistry Indian Institute of Technology, Kharagpur Lecture-11 Enzyme Mechanisms II

Biochemistry - I. Prof. S. Dasgupta Department of Chemistry Indian Institute of Technology, Kharagpur Lecture-11 Enzyme Mechanisms II Biochemistry - I Prof. S. Dasgupta Department of Chemistry Indian Institute of Technology, Kharagpur Lecture-11 Enzyme Mechanisms II In the last class we studied the enzyme mechanisms of ribonuclease A

More information

CHAPTER 3 THE CHEMISTRY OF ORGANIC MOLECULES

CHAPTER 3 THE CHEMISTRY OF ORGANIC MOLECULES CHAPTER 3 THE CHEMISTRY OF ORGANIC MOLECULES 3.1 Organic Molecules The chemistry of carbon accounts for the diversity of organic molecules found in living things. Carbon has six electrons, four of which

More information

4. Which carbohydrate would you find as part of a molecule of RNA? a. Galactose b. Deoxyribose c. Ribose d. Glucose

4. Which carbohydrate would you find as part of a molecule of RNA? a. Galactose b. Deoxyribose c. Ribose d. Glucose 1. How is a polymer formed from multiple monomers? a. From the growth of the chain of carbon atoms b. By the removal of an OH group and a hydrogen atom c. By the addition of an OH group and a hydrogen

More information

Chapter 5: The Structure and Function of Large Biological Molecules

Chapter 5: The Structure and Function of Large Biological Molecules Name Period Concept 5.1 Macromolecules are polymers, built from monomers 1. The large molecules of all living things fall into just four main classes. Name them. 2. Circle the three classes that are called

More information

H H N - C - C 2 R. Three possible forms (not counting R group) depending on ph

H H N - C - C 2 R. Three possible forms (not counting R group) depending on ph Amino acids - 0 common amino acids there are others found naturally but much less frequently - Common structure for amino acid - C, -N, and functional groups all attached to the alpha carbon N - C - C

More information

UNIT (11) MOLECULES OF LIFE: LIPIDS AND PROTEINS

UNIT (11) MOLECULES OF LIFE: LIPIDS AND PROTEINS UNIT (11) MOLECULES OF LIFE: LIPIDS AND PROTEINS 11.1 Types of Lipids Lipids are also biochemical compounds that contain carbon, hydrogen, and oxygen. But lipids, unlike carbohydrates, share no common

More information

AP BIOLOGY 2008 SCORING GUIDELINES

AP BIOLOGY 2008 SCORING GUIDELINES AP BIOLOGY 2008 SCORING GUIDELINES Question 1 1. The physical structure of a protein often reflects and affects its function. (a) Describe THREE types of chemical bonds/interactions found in proteins.

More information

Lecture Overview. Hydrogen Bonds. Special Properties of Water Molecules. Universal Solvent. ph Scale Illustrated. special properties of water

Lecture Overview. Hydrogen Bonds. Special Properties of Water Molecules. Universal Solvent. ph Scale Illustrated. special properties of water Lecture Overview special properties of water > water as a solvent > ph molecules of the cell > properties of carbon > carbohydrates > lipids > proteins > nucleic acids Hydrogen Bonds polarity of water

More information

PRACTICE TEST QUESTIONS

PRACTICE TEST QUESTIONS PART A: MULTIPLE CHOICE QUESTIONS PRACTICE TEST QUESTIONS DNA & PROTEIN SYNTHESIS B 1. One of the functions of DNA is to A. secrete vacuoles. B. make copies of itself. C. join amino acids to each other.

More information

2007 7.013 Problem Set 1 KEY

2007 7.013 Problem Set 1 KEY 2007 7.013 Problem Set 1 KEY Due before 5 PM on FRIDAY, February 16, 2007. Turn answers in to the box outside of 68-120. PLEASE WRITE YOUR ANSWERS ON THIS PRINTOUT. 1. Where in a eukaryotic cell do you

More information

This class deals with the fundamental structural features of proteins, which one can understand from the structure of amino acids, and how they are

This class deals with the fundamental structural features of proteins, which one can understand from the structure of amino acids, and how they are This class deals with the fundamental structural features of proteins, which one can understand from the structure of amino acids, and how they are put together. 1 A more detailed view of a single protein

More information

Invariant residue-a residue that is always conserved. It is assumed that these residues are essential to the structure or function of the protein.

Invariant residue-a residue that is always conserved. It is assumed that these residues are essential to the structure or function of the protein. Chapter 6 The amino acid side chains have polar and nonpolar properties, and the relative hydrophobicity of the amino acid side chains is critical for the folding and stability of a protein. The more hydrophobic

More information

Biochemistry 2000 Sample Question Proteins. (1) Identify the secondary structure described in each of the following statements:

Biochemistry 2000 Sample Question Proteins. (1) Identify the secondary structure described in each of the following statements: (1) Identify the secondary structure described in each of the following statements: a. A coiled peptide chain held in place by hydrogen bonding between peptide bonds in the same chain b. A structure that

More information

Proteins are polymers of amino acids. Protein-over 50 amino acids, peptide-under 50 amino acids.

Proteins are polymers of amino acids. Protein-over 50 amino acids, peptide-under 50 amino acids. Amino Acids and Proteins: Protein Functions: enzymes, transport (hemoglobin-o 2, tranferrin-fe), protection (MHC molecules, immunoglobulins), hormones (insulin, glucagons), gene transcription regulation

More information

Chapter 3: Biological Molecules. 1. Carbohydrates 2. Lipids 3. Proteins 4. Nucleic Acids

Chapter 3: Biological Molecules. 1. Carbohydrates 2. Lipids 3. Proteins 4. Nucleic Acids Chapter 3: Biological Molecules 1. Carbohydrates 2. Lipids 3. Proteins 4. Nucleic Acids Elements in Biological Molecules Biological macromolecules are made almost entirely of just 6 elements: Carbon (C)

More information

Polypeptides and Proteins

Polypeptides and Proteins Polypeptides and Proteins These molecules are composed, at least in part, of chains of amino acids. Each amino acid is joined to the next one through an amide or peptide bond from the carbonyl carbon of

More information

(Woods) Chem-131 Lec-20 & Proteins 1

(Woods) Chem-131 Lec-20 & Proteins 1 (Woods) Chem-131 Lec-20 & 22 09-4 Proteins 1 Catalytic proteins, or enzymes: Catalyze the synthesis and utilization of proteins, carbohydrates, lipids, nucleic acids, and almost all other biomolecules.

More information

Non-Covalent Bonds (Weak Bond)

Non-Covalent Bonds (Weak Bond) Non-Covalent Bonds (Weak Bond) Weak bonds are those forces of attraction that, in biological situations, do not take a large amount of energy to break. For example, hydrogen bonds are broken by energies

More information

Introduction to Protein Folding

Introduction to Protein Folding Introduction to Protein Folding Chapter 4 Proteins: Three Dimensional Structure and Function Conformation - three dimensional shape Native conformation - each protein folds into a single stable shape (physiological

More information

Proteins. Amino Acids. Chapter 3. Molecular Diagnostics Fundamentals, Methods and Clinical Applications Second Edition 2/5/2013

Proteins. Amino Acids. Chapter 3. Molecular Diagnostics Fundamentals, Methods and Clinical Applications Second Edition 2/5/2013 Proteins Chapter 3 Amino Acids Nonpolar Alanine, Ala, A Isoleucine, Ile, I Leucine, Leu, L Methionine, Met, M Phenylalanine, Phe, F Tryptophan,Trp, W Valine, Val, V Negatively Charged (Acidic) Aspartic

More information

Amino Acids, Peptides and Proteins

Amino Acids, Peptides and Proteins Amino Acids, Peptides and Proteins 1. α-amino Acids C (S) or L amino acids a) dipolar nature (isoelectric points) b) synthesis (racemic) i) from α-bromoacids ii) Strecker synthesis from aldehydes iii)

More information

The Molecules of Cells

The Molecules of Cells The Molecules of Cells I. Introduction A. Most of the world s population cannot digest milk-based foods. 1. These people are lactose intolerant because they lack the enzyme lactase. 2. This illustrates

More information

Protein Folding. Cell/mol bio lab. Proteins are like a long spaghetti noodle, folded back upon itself over and over

Protein Folding. Cell/mol bio lab. Proteins are like a long spaghetti noodle, folded back upon itself over and over Protein Folding Cell/mol bio lab Proteins are like a long spaghetti noodle, folded back upon itself over and over Why study the 3-D 3 D shape of a protein? (go to Cell Biology web site from my home page)

More information

A) at equilibrium B) endergonic C) endothermic D) exergonic E) exothermic

A) at equilibrium B) endergonic C) endothermic D) exergonic E) exothermic CHEM 2770: Elements of Biochemistry Mid Term EXAMINATION VERSION B Date: October 29, 2014 Instructor: H. Perreault Location: 172 Schultz Time: 4 or 6 pm. Duration: 1 hour Instructions Please mark the Answer

More information

MBLG1001_lecture 4 Page 1. University of Sydney Library Electronic Item COURSE: MBLG1001. Lecturer: Dale Hancock Forming the Protein

MBLG1001_lecture 4 Page 1. University of Sydney Library Electronic Item COURSE: MBLG1001. Lecturer: Dale Hancock Forming the Protein MBLG1001_lecture 4 Page 1 University of Sydney Library Electronic Item URSE: MBLG1001 Lecturer: Dale ancock Forming the Protein MMWEALT F AUSTRALIA opyright Regulation WARIG This material has been reproduced

More information

Properties of Proteins

Properties of Proteins Properties of Proteins Experiment #8 Objective: To study chemical and physical properties of proteins from natural sources (egg and milk) and some chemical reactions of amino acid residues in these proteins,

More information

Chapter 17 An Introduction to Organic Chemistry, Biochemistry, and Synthetic Polymers

Chapter 17 An Introduction to Organic Chemistry, Biochemistry, and Synthetic Polymers 263 Chapter 17 An Introduction to Organic Chemistry, Biochemistry, and Synthetic Polymers Review Skills 17.1 Organic Compounds Formulas for Organic Compounds Alkanes Alkenes Alkynes Arenes (Aromatics)

More information

Myoglobin and Hemoglobin

Myoglobin and Hemoglobin Myoglobin and Hemoglobin Myoglobin and hemoglobin are hemeproteins whose physiological importance is principally related to their ability to bind molecular oxygen. Myoglobin (Mb) The oxygen storage protein

More information

Activity 4/5.1 How Can You Identify Organic Macromolecules?

Activity 4/5.1 How Can You Identify Organic Macromolecules? Answers? Activity 4/5.1 ow an You Identify rganic Macromolecules? efer to the figure (Some Simple hemistry) on the next page when doing this activity. Part A. Answer the questions. Then use your answers

More information

Ms. Campbell Protein Synthesis Practice Questions Regents L.E.

Ms. Campbell Protein Synthesis Practice Questions Regents L.E. Name Student # Ms. Campbell Protein Synthesis Practice Questions Regents L.E. 1. A sequence of three nitrogenous bases in a messenger-rna molecule is known as a 1) codon 2) gene 3) polypeptide 4) nucleotide

More information

CSC 2427: Algorithms for Molecular Biology Spring 2006. Lecture 16 March 10

CSC 2427: Algorithms for Molecular Biology Spring 2006. Lecture 16 March 10 CSC 2427: Algorithms for Molecular Biology Spring 2006 Lecture 16 March 10 Lecturer: Michael Brudno Scribe: Jim Huang 16.1 Overview of proteins Proteins are long chains of amino acids (AA) which are produced

More information

Ionization of amino acids

Ionization of amino acids Amino Acids 20 common amino acids there are others found naturally but much less frequently Common structure for amino acid COOH, -NH 2, H and R functional groups all attached to the a carbon Ionization

More information

BNFO601 Introduction to Molecular Biology Protein

BNFO601 Introduction to Molecular Biology Protein BNFO601 Introduction to Molecular Biology Protein Outline: A. What can protein do? B. What are proteins? C. Structure and basis for catalysis D. Targeting protein E. Alteration of protein structure and

More information

Chemistry 20 Chapters 15 Enzymes

Chemistry 20 Chapters 15 Enzymes Chemistry 20 Chapters 15 Enzymes Enzymes: as a catalyst, an enzyme increases the rate of a reaction by changing the way a reaction takes place, but is itself not changed at the end of the reaction. An

More information

Solutions for Biochemistry Unit Exam

Solutions for Biochemistry Unit Exam Solutions for Biochemistry Unit Exam Question 1 a) An example of a structural representation is shown in the adjacent box. Draw a structural representation of the amino acid, Aspartic acid, which has the

More information

The Chapter Structure 5 and Function of Large Biological Molecules

The Chapter Structure 5 and Function of Large Biological Molecules Overview: The Molecules of Life The Chapter Structure 5 and Function of Large Biological Molecules The Structure and Function of Large Biological Molecules All living things are made up of four classes

More information

Folding of Proteins - Simulation using Monte Carlo Approach

Folding of Proteins - Simulation using Monte Carlo Approach A Report On Folding of Proteins - Simulation using Monte Carlo Approach Prepared By Ramji T. Venkatasubramanian In Partial fulfillment of course Computational Nanomechanics ME 8253 Spring Semester, May

More information

The peptide bond is rigid and planar

The peptide bond is rigid and planar Level Description Bonds Primary Sequence of amino acids in proteins Covalent (peptide bonds) Secondary Structural motifs in proteins: α- helix and β-sheet Hydrogen bonds (between NH and CO groups in backbone)

More information

Sickle cell anemia: Altered beta chain Single AA change (#6 Glu to Val) Consequence: Protein polymerizes Change in RBC shape ---> phenotypes

Sickle cell anemia: Altered beta chain Single AA change (#6 Glu to Val) Consequence: Protein polymerizes Change in RBC shape ---> phenotypes Protein Structure Polypeptide: Protein: Therefore: Example: Single chain of amino acids 1 or more polypeptide chains All polypeptides are proteins Some proteins contain >1 polypeptide Hemoglobin (O 2 binding

More information

Recognizing Organic Molecules: Carbohydrates, Lipids and Proteins

Recognizing Organic Molecules: Carbohydrates, Lipids and Proteins Recognizing Organic Molecules: Carbohydrates, Lipids and Proteins Oct 15 8:05 PM What is an Organic Molecule? An Organic Molecule is a molecule that contains carbon and hydrogen and oxygen Carbon is found

More information

GSAK YLDR WGSM. (b) (5 pts) Explain why neither of these steps alone is sufficient to unambiguously determine the sequence of your peptide.

GSAK YLDR WGSM. (b) (5 pts) Explain why neither of these steps alone is sufficient to unambiguously determine the sequence of your peptide. Problem 1. (total 30 points) You have to determine the amino acid sequence of a peptide. You performed the following steps using enzyme cleavage of your peptide (see table on the front page) combined with

More information

OBJECTIVES LECTURE: By the end of this lecture, student can:

OBJECTIVES LECTURE: By the end of this lecture, student can: PROTEIN By: Dr. Shamsul Azahari Zainal Badari Department of Resource Management and Consumer Studies Faculty of Human Ecology Universiti Putra Malaysia OBJECTIVES LECTURE: By the end of this lecture,

More information

Chapter 26 Biomolecules: Amino Acids, Peptides, and Proteins

Chapter 26 Biomolecules: Amino Acids, Peptides, and Proteins John E. McMurry www.cengage.com/chemistry/mcmurry Chapter 26 Biomolecules: Amino Acids, Peptides, and Proteins Proteins Amides from Amino Acids Amino acids contain a basic amino group and an acidic carboxyl

More information