IV. -Amino Acids: carboxyl and amino groups bonded to -Carbon. V. Polypeptides and Proteins
|
|
- Kathryn Jones
- 8 years ago
- Views:
Transcription
1 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 3 N+-C -COO- B. Ca is tetrahedral and bonded to 4 different groups 1. L configuration for all natural amino acids (few exceptions) different R groups C. Classification based on R-group - know one example from each 1. Aliphatic-hydrophobic 2. Aromatic-hydrophobic 3. Polar Uncharged-hydrophilic 4. Acidic-hydrophilic 5. B a s i c - hydrophilic V. Polypeptides and Proteins A. Peptide Bond 1. join amino group of one amino acid with carboxyl group of another by forming and amide bond between them! Peptide Bond 2. C-N bond has partial double bond character B. Peptides and Polypeptides 1. Peptides contain relatively few amino acids linked by peptide bonds: dipeptide, tripeptide, tetrapeptide,. 2. Polypeptide contains many amino acids and if there are very many amino acids one can call it protein C. Proteins have molecular weights > several thousand and have 3-4 levels of structure 1. Primary Structure (1 ) sequence of amino acids connected by peptide bonds 2. Secondary Structure (2 ) local conformation of peptide bond backbone stabilized by H-bonds: -helix: intrachain H-bonds & -sheet: interchain H-bonds 3. Tertiary Structure (3 ): The complete 3-dimensional structure described by the way the polypeptide chain folds back on itself; stabilized by interactions (bonds) between the amino acid R-groups. Hydrophobic Bonds & van der Walls Interactions most important 4. Quaternary Structure (4 ): only some proteins have 4 structure which is the association of more than one polypeptide
2 Monomer Monosaccharide (Sugar) Simple Polymer Oligosaccharide Complex Polymer (Macromolecule) Polysaccharide (Complex Carbohydrate) Nucleotide Oligonucleotide Nucleic Acid Amino Acid Peptide Polypeptide Protein
3 Table 5.1 An Overview of Protein Functions
4 Describing Macromolecular Structure
5 α-amino Acids α carbon Amino group Carboxyl group At low ph ph ~7 at high ph H + H 3 N C C O OH R - H + + H + H + H 3 N C C O O R - H + + H + H H 2 N C C O O R +1 Charge 0 Charge -1 Charge
6 Stereochemistry -- Tetrahedral α-carbon L-Alanine O C O α-carbon O C D-Alanine O N C C N C C
7 20 Different Amino Acids Are Found in Proteins 1-Letter Name 3-Letter 1-Letter Name 3-Letter A Alanine A M Methionine Met C Cysteine Cys N Asparagine Asn D Aspartic Acid Asp P Proline Pro E Glutamic Acid Glu Q Glutamine Gln F Phenylalanine Phe R Arginine Arg G Glycine G S Serine Set H Histidine H T Threonine Thr I Isoleucine Ile V Valine Val K Lysine Lys W Tryptophan Trp L Leucine Leu Y Tyrosine Tyr
8 Fig. 5.16a: Non-polar, hydrophobic aliphatic and aromatic amino acids often cluster together and are found in the interior of proteins Nonpolar side chains; hydrophobic Side chain Glycine (Gly or G) Alanine (Ala or A) Valine (Val or V) Leucine (Leu or L) Isoleucine (Ile or I) Methionine (Met or M) Phenylalanine (Phe or F) Tryptophan (Trp or W) Proline (Pro or P)
9 Fig. 5.16b: Polar uncharged side chains; hydrophilic Serine (Ser or S) Threonine (Thr or T) Cysteine (Cys or C) Tyrosine (Tyr or Y) Asparagine (Asn or N) Glutamine (Gln or Q)
10 Fig. 5.16b: Amino Acids with Hydroxyl Groups in their Sidechains (S, T, Y) These amino acids can also be modified by phosphorylation (addition of phosphate to the hydroxyl group) O - Side chain-o-h Side chain-o-p-o - O
11 Fig. 5.16b: Amino Acids with Hydroxyl Groups in their Sidechains (S, T, Y) O-PO 3 O-PO 3 These amino acids can also be modified by phosphorylation (addition of phosphate to the hydroxyl group) O - Side chain-o-h Side chain-o-p-o - O
12 Aspartic acid (Asp or D) Glutamic acid (Glu or E) Lysine (Lys or K) Arginine (Arg or R) Histidine (His or H)
13 Note: similar size and shape but different chemical properties Asparagine (Asn) N Aspartic Acid (Asp) D Glutamine (Gln) Q Glutamic Acid (Glu) E
14 Aromatic side chains (F,W,Y) Tyrosine (Tyr) Y Phenylalanine (Phe) F Tryptophan (Trp) W Ring system in side chain absorbs ultra-violet (UV) light giving us a way of measuring protein concentration Note similar size and shape of Tyr and Phe (only difference is extra OH group in Tyr making it more hydrophilic)
15 Special cases: Glycine (Gly) G Glycine is the smallest amino acid and its small side chain can fit into small spaces in protein Cysteine (Cys) C The sulfhydryl group (-S-H) of two cysteines can react to form a covalent disulfide bridge (-S-S-) Proline (Pro) P The side chain of proline is covalently linked back to the α-amino group. This limits the rotation of the side chain and introduces kinks in proteins
16 Amino Acids Whose Structures You Need to Know Alanine (Ala) Aliphatic hydrophobic Phenylalanine (Phe) Aromatic hydrophobic Serine (Ser) Polar uncharged Lysine (Lys) Basic Aspartic Acid (Asp) Acidic
17 Fig. 5.17: Peptide Bonds Link Amino Acids Peptide bond Side chains New peptide bond forming Backbone Amino end (N-terminus) Peptide bond Carboxyl end (C-terminus)
18 Peptide Bond: How proteins (polypeptides) are made from amino acids? H + H 3 N C C O OH R 1 O C C N C H H 2 O H H δ- O C α C N δ+ C α H H N C C O O - R 2 Lone electron pair on N forms second bond O - + C C N C H or O + H 3 N C C R 1 N C C O O - H R 2 The π bond is shared between the O and N in the Peptide Bond Group. Thus, each C=O and C=N bond behaves like a double bond, and there is no rotation around the bonds connecting these atoms. Furthermore, all of the atoms of the peptide bonding group lie on a plane. H H Amide bond O C C N C H The Peptide Bond group is Polar and Planar (the atoms lie on a plane)
19 Peptide Bond: Structural characteristics Peptide Bonds free rotation is not possible around C-O and C-N bonds. Rotation is possible around the single bonds to the C α s C α O C N H C α C O H N C α Planar Peptide Bond groups joined at C α s Side Chain Main Chain Amino Terminus Carboxy Terminus
20 Aspartame a.k.a. NutraSweet - Is a Dipeptide AspartylAlanineMethylEster, a dipeptide. It is shown in two orientations to demonstrate the 120 bond angles between between the atoms of the peptide bond, and the fact that all of these atoms lie on a plane. 120
21 Secondary Structure: Local folding of the polypeptide backbone 1.5 Å Hydrogen Bond 3.6 residues/turn 5.4 Å Hydrogen Bond.5 Å
22 Fig. 5.18: Tertiary Structure Describes overall fold of polypeptide backbone β-sheet α-helices Folding puts some amino acid side chains (Hydrophobic) in interior and some (Hydrophilic) on exterior surface of protein Different functional groups on surface give local sites distinct shapes and specific properties
23 Fig. 5.20: What Bonds Stabilize Tertiary Structure? 1. Hydrophobic and van derwaals Interactions: Packing (clustering) of hydrophobic side chains into interior away from water, keeping most hydrophilic side chains on surface. 2. Hydrogen bonds of secondary structure elements 3. Ionic interactions between oppositely charged side chains 4. Some proteins are also stabilized by disulfide bonds between pairs of cysteine side chains
24 Fig. 5.21: The Four Levels of Protein Structure Primary Structure Secondary Structure Tertiary Structure Quaternary Structure + H 3 N Amino end β pleated sheet Examples of amino acid subunits α helix
25 Level of Structure Type of Bond Between peptide bond groups Hydrophobic Bond most important + others
26 Fig. 5.22: Changing A Proteins s Amino Acid Sequence Can Change Its Shape Sickle-cell hemoglobin Normal hemoglobin Primary Structure Secondary and Tertiary Structures β subunit Exposed hydrophobic region β subunit α β α β Quaternary Structure Normal hemoglobin Sickle-cell hemoglobin β α β α Function Molecules do not associate with one another; each carries oxygen. Molecules crystallize into a fiber; capacity to carry oxygen is reduced. Red Blood Cell Shape 10 µm 10 µm
27 Fig. 5.23: Amino Acid (primary structure) Sequence Determines Shape Anfinsen experiment (1965) Denaturation (Unfolding) increase temperature, change ph, add chemical agents that disrupt hydrogen bonds, ionic bonds and disulfide bridges Normal protein (Biologically active) Folding (spontaneous) Renaturation Denatured protein (Biologically inactive)
28 Proteins Form a Variety of Shapes and Sizes
29 Quaternary Structure: Some proteins form stable oligomeric structures containing two or more polypeptides Hemoglobin Antibodies Photosynthetic Reaction Center (membrane protein)
30 Membrane Proteins: Some are a single polypeptide others have Quaternary Structure Bacteriorhodopsin Photosynthetic Reaction Center (membrane protein) Bacterial Porin
31 Cofactors: Some proteins bind ions and/or organic molecules to help them fulfill their function Hemoglobin Myoglobin
32 Molecules that interact stably have complementary shapes (fit like a lock-and-key or a hand in a glove) so that they can make lots of weak intermolecular bonds
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 informationPipe 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 informationAmino 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 informationPart 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 informationA. 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 informationBOC334 (Proteomics) Practical 1. Calculating the charge of proteins
BC334 (Proteomics) Practical 1 Calculating the charge of proteins Aliphatic amino acids (VAGLIP) N H 2 H Glycine, Gly, G no charge Hydrophobicity = 0.67 MW 57Da pk a CH = 2.35 pk a NH 2 = 9.6 pi=5.97 CH
More informationShu-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 informationThe 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 informationAmino 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 informationRecap. 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 informationPaper: 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 informationPeptide bonds: resonance structure. Properties of proteins: Peptide bonds and side chains. Dihedral angles. Peptide bond. Protein physics, Lecture 5
Protein physics, Lecture 5 Peptide bonds: resonance structure Properties of proteins: Peptide bonds and side chains Proteins are linear polymers However, the peptide binds and side chains restrict conformational
More informationCarbohydrates, 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 informationProtein 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 informationBuilt 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 informationStructure 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 informationIonization 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 information18.2 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 informationAmino Acids. Amino acids are the building blocks of proteins. All AA s have the same basic structure: Side Chain. Alpha Carbon. Carboxyl. Group.
Protein Structure Amino Acids Amino acids are the building blocks of proteins. All AA s have the same basic structure: Side Chain Alpha Carbon Amino Group Carboxyl Group Amino Acid Properties There are
More informationH 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 informationCh18_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 informationAmino Acids, Proteins, and Enzymes. Primary and Secondary Structure Tertiary and Quaternary Structure Protein Hydrolysis and Denaturation
Amino Acids, Proteins, and Enzymes Primary and Secondary Structure Tertiary and Quaternary Structure Protein Hydrolysis and Denaturation 1 Primary Structure of Proteins H 3 N The particular sequence of
More informationThe 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 informationINTRODUCTION 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 informationChemistry 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 informationChapter 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 information8/20/2012 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 informationPeptide 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 informationStructure 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 informationChapter 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 informationProteins. 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 informationCHAPTER 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 informationAMINO ACIDS & PEPTIDE BONDS STRUCTURE, CLASSIFICATION & METABOLISM
AMINO ACIDS & PEPTIDE BONDS STRUCTURE, CLASSIFICATION & METABOLISM OBJECTIVES At the end of this session the student should be able to, recognize the structures of the protein amino acid and state their
More informationChapter 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 information4. 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 informationTHE CHEMICAL SYNTHESIS OF PEPTIDES
TE EMIAL SYTESIS F PEPTIDES Peptides are the long molecular chains that make up proteins. Synthetic peptides are used either as drugs (as they are biologically active) or in the diagnosis of disease. Peptides
More informationA 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 informationBiological 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 information2007 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 informationMCAT 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 informationExam 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 informationLecture 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 informationNafith 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 informationHow To Understand 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 informationCombinatorial Biochemistry and Phage Display
Combinatorial Biochemistry and Phage Display Prof. Valery A. Petrenko Director - Valery Petrenko Instructors Galina Kouzmitcheva and I-Hsuan Chen Auburn 2006, Spring semester COMBINATORIAL BIOCHEMISTRY
More information(c) How would your answers to problem (a) change if the molecular weight of the protein was 100,000 Dalton?
Problem 1. (12 points total, 4 points each) The molecular weight of an unspecified protein, at physiological conditions, is 70,000 Dalton, as determined by sedimentation equilibrium measurements and by
More informationChapter 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 informationIntroduction to Chemical Biology
Professor Stuart Conway Introduction to Chemical Biology University of xford Introduction to Chemical Biology ecommended books: Professor Stuart Conway Department of Chemistry, Chemistry esearch Laboratory,
More informationCSC 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 informationChapter 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 informationDisaccharides 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 informationThe peptide bond Peptides and proteins are linear polymers of amino acids. The amino acids are
Introduction to Protein Structure Proteins are large heteropolymers usually comprised of 50 2500 monomer units, although larger proteins are observed 7. The monomer units of proteins are amino acids. The
More informationChapter 2: Biochemistry Problems
hapter 2: Biochemistry Problems Biochemistry Problems If you were a biochemist, you would study chemical substances and vital processes that occur in living organisms. You might study macromolecules such
More informationPreviously published in Biophysical Society On-line Textbook PROTEINS CHAPTER 1. PROTEIN STRUCTURE. Section 1. Primary structure, secondary motifs,
Previously published in Biophysical Society On-line Textbook PROTEINS CHAPTER 1. PROTEIN STRUCTURE Section 1. Primary structure, secondary motifs, tertiary architecture, and quaternary organization Jannette
More informationIn addition to being shorter than a single bond, the double bonds in ethylene don t twist the way single bonds do. In other words, the other atoms
In addition to being shorter than a single bond, the double bonds in ethylene don t twist the way single bonds do. In other words, the other atoms attached to the carbons (hydrogens in this case) can no
More informationProteins 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 informationNO CALCULATORS OR CELL PHONES ALLOWED
Biol 205 Exam 1 TEST FORM A Spring 2008 NAME Fill out both sides of the Scantron Sheet. On Side 2 be sure to indicate that you have TEST FORM A The answers to Part I should be placed on the SCANTRON SHEET.
More informationBiochemistry - 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 informationHelices 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 informationThis 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 informationMyoglobin 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 informationChapter 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 informationThe 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 informationI 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 informationChemical Basis of Life Module A Anchor 2
Chemical Basis of Life Module A Anchor 2 Key Concepts: - Water is a polar molecule. Therefore, it is able to form multiple hydrogen bonds, which account for many of its special properties. - Water s polarity
More informationPROTEINS STRUCTURE AND FUNCTION (DR. TRAISH)
Introduction to Proteins - Proteins are abundant and functionally diverse molecules - They participate in cell regulation at all levels - They share a common structural feature: all are linear polymers
More informationChapter 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 informationDisulfide 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 informationLecture 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 informationElements in Biological Molecules
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 informationAmino Acids as Acids, Bases and Buffers:
Amino Acids as Acids, Bases and Buffers: - Amino acids are weak acids - All have at least 2 titratable protons (shown below as fully protonated species) and therefore have 2 pka s o α-carboxyl (-COOH)
More informationProtein Structure and Function
Jones & Bartlett Learning, LL. T F SALE DISTIBUTI Protein Structure and Function SETI I APTE 2 APTE 3 Protein Structure Protein Function 27 Jones & Bartlett Learning, LL. T F SALE DISTIBUTI 2 Protein Structure
More informationPreliminary MFM Quiz
Preliminary MFM Quiz 1. The major carrier of chemical energy in all cells is: A) adenosine monophosphate B) adenosine diphosphate C) adenosine trisphosphate D) guanosine trisphosphate E) carbamoyl phosphate
More informationUNIT (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 informationInvariant 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 informationMolecular Facts and Figures
Nucleic Acids Molecular Facts and Figures DNA/RNA bases: DNA and RNA are composed of four bases each. In DNA the four are Adenine (A), Thymidine (T), Cytosine (C), and Guanine (G). In RNA the four are
More informationGuidelines for Writing a Scientific Paper
Guidelines for Writing a Scientific Paper Writing an effective scientific paper is not easy. A good rule of thumb is to write as if your paper will be read by a person who knows about the field in general
More informationStructures 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 informationCovalent bonds are the strongest chemical bonds contributing to the protein structure A peptide bond is formed between with of the following?
MCAT Question Covalent bonds are the strongest chemical bonds contributing to the protein structure A peptide bond is formed between with of the following? A. Carboxylic group and amino group B. Two carboxylic
More informationhttp://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 informationAP 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 informationNon-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 informationBiological molecules:
Biological molecules: All are organic (based on carbon). Monomers vs. polymers: Monomers refer to the subunits that, when polymerized, make up a larger polymer. Monomers may function on their own in some
More informationProteins 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 informationConformational 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 informationPeptides & Proteins. (thanks to Hans Börner)
Peptides & Proteins (thanks to Hans Börner) 1 Proteins & Peptides Proteuos: Proteus (Gr. mythological figure who could change form) proteuo: "first, ref. the basic constituents of all living cells peptos:
More informationPeptide Bonds: Structure
Peptide Bonds: Structure Peptide primary structure The amino acid sequence, from - to C-terminus, determines the primary structure of a peptide or protein. The amino acids are linked through amide or peptide
More informationLecture 4: Peptides and Protein Primary Structure [PDF] Key Concepts. Objectives See also posted Peptide/pH/Ionization practice problems.
Lecture 4: Peptides and Protein Primary Structure [PDF] Reading: Berg, Tymoczko & Stryer, Chapter 2, pp. 34-37 Practice problems (peptide ionization) [PDF]; problems in textbook: chapter 2, pp. 63-64,
More informationSickle 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 informationAcidic amino acids: Those whose side chains can carry a negative charge at certain ph values. Typically aspartic acid, glutamic acid.
A Acidic amino acids: Those whose side chains can carry a negative charge at certain ph values. Typically aspartic acid, glutamic acid. Active site: Usually applied to catalytic site of an enzyme or where
More informationFrom Sequence to Structure
1 From Sequence to Structure The genomics revolution is providing gene sequences in exponentially increasing numbers. onverting this sequence information into functional information for the gene products
More informationLab 3 Organic Molecules of Biological Importance
Name Biology 3 ID Number Lab 3 Organic Molecules of Biological Importance Section 1 - Organic Molecules Section 2 - Functional Groups Section 3 - From Building Blocks to Macromolecules Section 4 - Carbohydrates
More informationBiochemistry of Cells
Biochemistry of Cells 1 Carbon-based Molecules Although a cell is mostly water, the rest of the cell consists mostly of carbon-based molecules Organic chemistry is the study of carbon compounds Carbon
More informationPeptide Design Strategy: Basics, Optimization, and Application. Presented by: Tiffany Gupton Campolongo, Ph.D.
Peptide Design Strategy: Basics, Optimization, and Application Presented by: Tiffany Gupton Campolongo, Ph.D. Presentation overview 1 2 3 4 Introduction Peptide Design Basics Advanced Design Strategy Strategy
More informationChapter 2 Chemical Principles
Chapter 2 Chemical Principles I. Chemistry. [Students should read this section on their own]. a. Chemistry is the study of the interactions between atoms and molecules. b. The atom is the smallest unit
More informationThe chemistry of insulin
FREDERICK S ANGER The chemistry of insulin Nobel Lecture, December 11, 1958 It is great pleasure and privilege for me to give an account of my work on protein structure and I am deeply sensitive of the
More informationConcluding lesson. Student manual. What kind of protein are you? (Basic)
Concluding lesson Student manual What kind of protein are you? (Basic) Part 1 The hereditary material of an organism is stored in a coded way on the DNA. This code consists of four different nucleotides:
More informationI. Chapter 5 Summary. II. Nucleotides & Nucleic Acids. III. Lipids
I. Chapter 5 Summary A. Simple Sugars (CH 2 O) n : 1. One C contains a carbonyl (C=O) rest contain - 2. Classification by functional group: aldoses & ketoses 3. Classification by number of C's: trioses,
More informationHydrogen Bonds The electrostatic nature of hydrogen bonds
Hydrogen Bonds Hydrogen bonds have played an incredibly important role in the history of structural biology. Both the structure of DNA and of protein a-helices and b-sheets were predicted based largely
More informationWORKING WITH PEPTIDES
WORKING WITH PEPTIDES 1 Synthetic custom peptides offer an increasingly affordable approach for exploring protein-protein interactions and more complex phenomena such as immune responses directed against
More information