C Cys Cysteine Cysteine is a small till intermediately large hydrophobic residue. It doesn t like the alpha helix, but doesn t mind strand and turn. I
|
|
- Marilyn Sims
- 7 years ago
- Views:
Transcription
1 A Ala Alanine Alanine is a small, hydrophobic residue. Its side chain, R, is just a methyl group. Alanine likes to sit in an alpha helix,it doesn t like beta strand very much, but it hates beta-turns. If you want to mutate a residue, but you don t have a good plan about what to replace it with, take alanine.
2 C Cys Cysteine Cysteine is a small till intermediately large hydrophobic residue. It doesn t like the alpha helix, but doesn t mind strand and turn. It can form Cys-Cys bridges with other cysteines. It can bind metals (especially Zn and Cu). The S-H group is very reactive.
3 D Asp Aspartic acid Aspartic acid, or aspartate, is an intermediately large, hydrophilic, negatively charged residue. Its side chain normally titrates at ph 4.5. It likes to sit near the N-terminus of a helix, and in turns. It hates strands.it often occurs in active sites. It can bind ions (mainly Ca).
4 E Glu Glutamic acid Glutamic acid, or glutamate, is a large, hydrophilic, negatively charged residue. Its side chain titrates at ph 4.6. It loves the helix, doesn t mind being in a strand, but is not so good for a turn.
5 F Phe Phenylalanine Phenylalanine is a large, hydrophobic, aromatic residue. It is good for a strand, it doesn t mind sitting in a helix, but it hates the turn.
6 G Gly Glycine Glycine is the smallest residue. It doesn t have a side chain, so its hydrophobicity is a bit undetermined, but you can call it hydrophobic or assign it an intermediate hydrophobicity. The fact that it doesn t have a side chain means that its backbone is very flexible so that it can make backbone turns that other residues cannot make. It is very bad for helix, bad for strand, but it is the star of the turns.
7 H His Histidine Histidine is very special. It is hydrophilic due to the two nitrogens in its side chain. Both nitrogens can titrate (the first one at ph 6.2). It is a little bit aromatic. It is often seen in active sites.it is neutral at physiological ph, but it can easily become positive, and occasionally even negative. It can bind metal ions (mainly Zn, Ni, Cu). It is not particularly picky about its secondary structure.
8 I Ile Isoleucine Isoleucine is an intermediately large, hydrophobic residue. It is beta branched which means that it likes to sit in a strand. It doesn t mind sitting in a helix either, but it cries its eyes out in a turn.
9 K Lys Lysine Lysine is a large, hydrophilic, positively charged residue. It is not a good strand residue, but it doesn t mind sitting in a helix or in a turn. Its side chain is very long and flexible.
10 L Leu Leucine Leucine is an intermediately large, hydrophobic residue that really loves to sit in a helix. It is also good for a strand, but it hates turns.
11 M Met Methionine Methionine is a large, sulphur containing, hydrophobic residue. It loves helices, doesn t mind sitting in a strand, but it hates turns. Methionine can bind metals with its sulphur, but this sulphur is much less reactive than the sulphur in cysteine. It is often the first residue of a molecule. The N-terminus is mostly positive and thus mostly at the surface. Therefore, methionine, despite being hydrophobic, is often at the surface. We call this a forced marriage.
12 N Asn Asparagine Asparagine is an intermediately large, polar residue. It hates the helix, is mildly un-amused in a strand, but it loves the turn. It can bind metal ions (Ca), but doesn t do that as well as its isosteric partner aspartic acid.
13 P Pro Proline In proline, the side chain is connected to the backbone at two places: the Cα and the N. Therefore, it is not an amino acid, but an imino acid. Unless it is the N-terminal residue, proline does not have a backbone proton, and thus is not good for helices and strands. Due to the extra covalent bond, proline is already pre-bend, and thus good for turns. Even though it is very hydrophobic, it often sits at the surface
14 Q Gln Glutamine Glutamine is a large, polar residue. It is not very picky about its secondary structure. It is isosteric with glutamic acid.
15 R Arg Arginine Arginine is a big, hydrophilic, positively charged residue. Its side chain contains a so-called guadinium group that is rigid. It is not picky about its secondary structure.
16 S Ser Serine Serine is a small, alcoholic residue of intermediate hydrophobicity. It is not too happy in helices and strands, but it loves to sit in turns. It often forms the active site of an enzyme together with histidine and aspartic acid. It is occasionally involved in metal (Ca) binding.
17 T Thr Threonine Threonine is a small, alcoholic residue of intermediate hydrophobicity. It is betabranched and thus good for beta strands. It doesn t care about helices or turns. It is occasionally involved in metal (Ca) binding.
18 V Val Valine Valine is a small hydrophobic residue. It is beta-branched and thus good for beta strands. It is isosteric with threonine. Valine doesn t care about helices, but it hates turns.
19 W Trp Tryptophan Tryptophan is the biggest residue. It is aromatic. Despite that the nitrogen in the five-ring is donor for hydrogen bonds, it is very hydrophobic. It doesn t care about helices or turns, but it loves strands.
20 Y Tyr Tyrosine Tyrosine is a large, aromatic, alcoholic residue of intermediate hydrophobicity. It is not so happy in a helix, indifferent about turns, and it loves a strand.
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 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 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 informationIV. -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 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 informationAdvanced 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 informationAmino Acid Properties and Consequences of Substitutions
Bioinformatics for Geneticists. Edited by Michael R. Barnes and Ian C. Gray Copyright 2003 John Wiley & Sons, Ltd. ISBNs: 0-470-84393-4 (HB); 0-470-84394-2 (PB) CHAPTER 14 Amino Acid Properties and Consequences
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 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 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 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 informationUNIVERSITETET I OSLO Det matematisk-naturvitenskapelige fakultet
1 UNIVERSITETET I OSLO Det matematisk-naturvitenskapelige fakultet Exam in: MBV4010 Arbeidsmetoder i molekylærbiologi og biokjemi I MBV4010 Methods in molecular biology and biochemistry I Day of exam:.
More informationApplication Note. Determination of 17 AQC derivatized Amino acids in baby food samples. Summary. Introduction. Category Bio science, food Matrix
Application Note Determination of 17 AQC derivatized Amino acids in baby food samples Category Bio science, food Matrix Baby food Method UHPLC Keywords Proteinogenic amino acids, canonical amino acids,
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 informationJournal of Chemical and Pharmaceutical Research
Available on line www.jocpr.com Journal of Chemical and Pharmaceutical Research J. Chem. Pharm. Res., 2010, 2(2): 372-380 ISSN No: 0975-7384 Determination of amino acid without derivatization by using
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 informationPet Enzyme lesson plan
Pet Enzyme lesson plan Introduction A. Enzymes as catalysts 1. Reactions may be thermodynamically favorable but not spontaneous 2. Kinetics/ and Ea of activation 3. Activation energy plot 4. Enzymes lower
More informationPrevious lecture: Today:
Previous lecture: The energy requiring step from substrate to transition state is an energy barrier called the free energy of activation G Transition state is the unstable (10-13 seconds) highest energy
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 informationINFORMATIKA ANGOL NYELVEN INFORMATION TECHNOLOGY
ÉRETTSÉGI VIZSGA 2006. május 17. INFORMATIKA ANGOL NYELVEN INFORMATION TECHNOLOGY 2006. május 17. 8:00 EMELT SZINTŰ GYAKORLATI VIZSGA ADVANCED LEVEL PRACTICAL EXAM A gyakorlati vizsga időtartama: 240 perc
More informationCopyright 2000-2003 Mark Brandt, Ph.D. 35
Amino acid breakdown Amino acids comprise one of the three major energy sources for animals. They are an especially important energy source for carnivorous animals, and for all animals during early starvation
More informationChapter 9. Applications of probability. 9.1 The genetic code
Chapter 9 Applications of probability In this chapter we use the tools of elementary probability to investigate problems of several kinds. First, we study the language of life by focusing on the universal
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 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 informationHuman Tubal Fluid (HTF) Media & Modifi ed Human Tubal Fluid (mhtf) Medium with Gentamicin
Human Tubal Fluid (HTF) Media & Modifi ed Human Tubal Fluid (mhtf) Medium with Gentamicin HTF Media are intended for use in assisted reproductive procedures which include gamete and embryo manipulation
More informationApplication Note. Determination of Amino acids by UHPLC with automated OPA- Derivatization by the Autosampler. Summary. Fig. 1.
Application Note Determination of Amino acids by UHPLC with automated PA- Derivatization by the Autosampler Category Bio Analysis Matrix - Method UHPLC Keywords Proteinogenic Amino acids, Canonical Amino
More informationLecture 15: Enzymes & Kinetics Mechanisms
ROLE OF THE TRANSITION STATE Lecture 15: Enzymes & Kinetics Mechanisms Consider the reaction: H-O-H + Cl - H-O δ- H Cl δ- HO - + H-Cl Reactants Transition state Products Margaret A. Daugherty Fall 2004
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 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 informationCHAPTER 15: ANSWERS TO SELECTED PROBLEMS
CHAPTER 15: ANSWERS T SELECTED PRBLEMS SAMPLE PRBLEMS ( Try it yourself ) 15.1 ur bodies can carry out the second reaction, because it requires less energy than we get from breaking down a molecule of
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 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 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 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 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 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 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 informationPRACTICE 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 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 informationBiochemistry 462a Hemoglobin Structure and Function Reading - Chapter 7 Practice problems - Chapter 7: 1-6; Proteins extra problems
Biochemistry 462a Hemoglobin Structure and Function Reading - Chapter 7 Practice problems - Chapter 7: 1-6; Proteins extra problems Myoglobin and Hemoglobin Oxygen is required for oxidative metabolism
More informationPatrick, An Introduction to Medicinal Chemistry 4e Chapter 13 Drug design: optimizing target interactions. Pyrrole ring N H
Patrick, An Introduction to dicinal hemistry 4e hapter 13 Drug design: optimizing target interactions Answers to end-of-chapter questions 1) The pyrrole ring of DU 122290 serves to increase the rigidity
More informationActual Quiz 1 (closed book) will be given Monday10/4 at 10:00 am
MIT Biology Department 7.012: Introductory Biology Fall 2004 Instructors: Professor Eric Lander, Professor Robert A. Weinberg, Dr. laudette Gardel 7.012 Practice Quiz 1 Actual Quiz 1 (closed book) will
More informationAmino Acids: An Introduction to Their Structure, Functions and Biochemical Properties
Amino Acids: An Introduction to Their Structure, Functions and Biochemical Properties Introduction Any time one deals with anything in Biology, one must also contend with amino acids and proteins: the
More informationHEMOGLOBIN AND MYOGLOBIN
HEMOGLOBIN AND MYOGLOBIN I. OXYGEN CARRIERS A. Why do we need oxygen carriers? i. Cannot carry enough in blood to meet metabolic demand ii. Oxygen is very reactive oxidizes iii. Oxygen cannot diffuse very
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 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 informationTranscription and Translation These terms describe the two steps used to transform the information carried in genes into useful products.
ranscription and ranslation hese terms describe the two steps used to transform the information carried in genes into useful products. he final product of some genes are R molecules. D ranscription R he
More informationAcute and Chronic Supplementation. Amino Acid
Introduction Acute and Chronic Supplementation of Amino Acids Eric R. Braverman, M.D. 1 and S. Lamola, B.S. 1 Of the four essential nutrient groups, amino acids may be the most fundamental to brain chemistry.
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 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 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 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 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 informationSecondary Structure Prediction. Michael Tress CNIO
Secondary Structure Prediction Michael Tress CNIO Why do we Need to Know About Secondary Structure? Secondary structure prediction is a step towards deducing the fold. In order to arrive at the correct
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 informationENZYMES. Serine Proteases Chymotrypsin, Trypsin, Elastase, Subtisisin. Principle of Enzyme Catalysis
ENZYMES Serine Proteases Chymotrypsin, Trypsin, Elastase, Subtisisin Principle of Enzyme Catalysis Linus Pauling (1946) formulated the first basic principle of enzyme catalysis Enzyme increase the rate
More informationRNA and Protein Synthesis
Name lass Date RN and Protein Synthesis Information and Heredity Q: How does information fl ow from DN to RN to direct the synthesis of proteins? 13.1 What is RN? WHT I KNOW SMPLE NSWER: RN is a nucleic
More informationAMINO ACIDS QUANTITATION IN BIOLOGICAL MEDIA. Monica Culea
STUDIA UNIVERSITATIS BABEŞ BLYAI, PHYSICA, L, 4b, 25 AMIN ACIDS QUANTITATIN IN BILGICAL MEDIA Monica Culea Univ. Babes Bolyai, Biomedical Physics Dept., 1 Kogalniceanu str, 34 Cluj Napoca, Romania e mail:
More informationAMINO ACIDS, PEPTIDES, AND PROTEINS
3 chapter + + AMI AIDS, PEPTIDES, AD PRTEIS 3.1 Amino Acids 75 3.2 Peptides and Proteins 85 3.3 Working with Proteins 89 3.4 The ovalent Structure of Proteins 96 3.5 Protein Sequences and Evolution 106
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 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 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 informationValidation of an HPLC method for the determination of amino acids in feed
J. Serb. Chem. Soc. 78 (6) 839 850 (2013) UDC 547.466+543.544.5.068.7:641.3.002.2 JSCS 4462 Original scientific paper Validation of an HPLC method for the determination of amino acids in feed IGOR JAJIĆ
More informationMultiple Choice Write the letter that best answers the question or completes the statement on the line provided.
Name lass Date hapter 12 DN and RN hapter Test Multiple hoice Write the letter that best answers the question or completes the statement on the line provided. Pearson Education, Inc. ll rights reserved.
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 informationAmino Acid Degradation
Amino Acid Degradation April 14, 2003 Bryant Miles The carbon skeletons of amino acids are broken down into metabolites that can either be oxidized into 2 and H 2 to generate ATP, or can be used for gluconeogenesis.
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 informationMs. 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 informationProtein. Protein. Why is protein important?
Protein Protein Though protein is often perceived as an area of concern for vegans, it is actually very easily accessible on a vegan diet, particularly if a variety of plant foods are consumed regularly.
More informationsystems AAA-Direct Amino Acid Analysis System
systems AAA-Direct Amino Acid Analysis System The Dionex AAA-Direct Amino Acid Analysis System revolutionizes the determination of amino acids. Unlike existing methods, amino acids are detected directly,
More informationNon-Ribosomal Peptide Synthesis
on-ibosomal Peptide Synthesis In contrast to proteins produced by ribosomal synthesis, many small peptide natural products contain not only the common 20 amino acids but also hundreds of different amino
More informationAnalysis of 25 underivatized amino acids in human plasma using ion-pairing reversed-phase liquid chromatography/time-of-flight mass spectrometry
RAPID COMMUNICATIONS IN MASS SPECTROMETRY Rapid Commun. Mass Spectrom. 2007; 21: 2717 2726 Published online in Wiley InterScience (www.interscience.wiley.com).3124 Analysis of 25 underivatized amino acids
More informationGeneral Protein Metabolism
General Protein Metabolism Protein Digestion Dietary proteins are very large complex molecules that cannot be absorbed from the intestine. To be absorbed, dietary proteins must be digested to small simple
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 informationRefinement of a pdb-structure and Convert
Refinement of a pdb-structure and Convert A. Search for a pdb with the closest sequence to your protein of interest. B. Choose the most suitable entry (or several entries). C. Convert and resolve errors
More informationThe three kinds of polymers that are prevalent in nature are
23 Amino Acids, Peptides, and Proteins The three kinds of polymers that are prevalent in nature are polysaccharides, proteins, and nucleic acids. You have already learned about polysaccharides, which are
More informationEnzymes reduce the activation energy
Enzymes reduce the activation energy Transition state is an unstable transitory combination of reactant molecules which occurs at the potential energy maximum (free energy maximum). Note - the ΔG of the
More information