BOC334 (Proteomics) Practical 1. Calculating the charge of proteins
|
|
|
- Alexandrina Eustacia Bryan
- 8 years ago
- Views:
Transcription
1 BC334 (Proteomics) Practical 1 Calculating the charge of proteins
2 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 3 H Alanine, Ala, A no charge Hydrophobicity = 1.0 MW 71Da pk a CH = 2.34 pk a NH 2 = 9.69 pi = 6.01 H 3 C CH 3 H Valine, Val, V no charge Hydrophobicity = 2.3 MW 99Da pk a CH = 2.32 pk a NH 2 = 9.62 pi = 5.97 C H 3 CH 3 H Leucine, Leu, L no charge Hydrophobicity = 2.2 MW 113Da pk a CH = 2.36 pk a NH 2 = 9.60 pi = 5.98 CH 3 CH 3 H Isoleucine, Ile, I no charge Hydrophobicity = 3.1 MW 113Da pk a CH = 2.36 pk a NH 2 = 9.68 pi = 6.02 H N H Proline, Pro, P no charge Hydrophobicity = MW 97Da pk a CH = 1.99 pk a NH 2 = pi = 6.48
3 Aromatic amino acids (FYW) N H 2 H Phenylalanine, Phe, F no charge Hydrophobicity = 2.5 Absorbs UV MW 147Da pk a CH = 1.83 pk a NH 2 = 9.13 pi=5.48 H H Tyrosine, Tyr, Y weak charge Hydrophobicity = 0.08 Absorbs UV MW 163Da pk a CH = 2.20 pk a NH 2 = 9.11 pi=5.66 NH H Tryptophan, Trp, W no charge Hydrophobicity = 1.5 Absorbs UV MW 186Da pk a CH = 2.38 pk a NH 2 = 9.39 pi=5.89
4 Polar but uncharged (SNQT) H H Serine, Ser, S no charge Hydrophobicity = -1.1 MW 87Da pk a CH = 2.21 pk a NH 2 = 9.15 pi = 5.68 H CH 3 H Threonine, Thr, T no charge Hydrophobicity = MW 101Da pk a CH = 2.11 pk a NH 2 = 9.62 pi = 5.87 N H 2 NH 2 H Asparagine, Asn, N no charge Hydrophobicity = -2.7 MW 114Da pk a CH = 2.02 pk a NH 2 = 8.08 pi = 5.41 N H 2 NH 2 H Glutamine, Gln, Q no charge Hydrophobicity = -2.9 MW 128Da pk a CH = 2.17 pk a NH 2 = 9.13 pi = 5.65
5 Sulphur containing (CM) HS H Cysteine, Cys, C weak charge Hydrophobicity = 0.17 MW 103Da pk a CH = 1.96 pk a NH 2 = 8.18 pi = 5.07 H 3 C S H Methionine, Met, M no charge Hydrophobicity = 1.1 MW 131Da pk a CH = 2.28 pk a NH 2 = 9.21 pi = 5.74
6 Charged (DEHKR) Acidic H H Aspartic acid, Asp, D negative charge Hydrophobicity = -3.0 MW 115Da pk a CH = 2.19 pk a NH 2 = 9.60 pi = 2.77 H H Glutamic acid, Glu, E negative charge Hydrophobicity = -2.6 MW 129Da pk a CH = 2.19 pk a NH 2 = 9.67 pi = 3.22 Basic HN N H Histidine, His, H Weak positive charge Hydrophobicity = -1.7 MW 137Da pk a CH = 1.82 pk a NH 2 = 9.17 pi = 7.59 H Lysine, Lys, K positive charge Hydrophobicity = -4.6 MW 128Da pk a CH = 2.18 pk a NH 2 = 8.95 pi = 9.47 HN N H 2 H Arginine, Arg, R positive charge Hydrophobicity = -7.5 MW 156Da pk a CH = 2.17 pk a NH 2 = 9.04 pi = NH 2 HN NH 2
7 Proteins have charges Ribbon Electrostatic surface
8 Histone H3 binds to DNA Histone H3 (ribbon) Histone H3 (electrostatic surface)
9 Nucleosome assembly protein (NAP1) binds to histones NAP1 (ribbon) NAP1 (electrostatic surface)
10 What charge is a protein? Depends on the ph The nature of the amino acids constituting the protein Each amino acid may contribute a specific fractional charge at a given ph The charge of the amino acid is given by the degree of dissociation of dissociable protons at the given ph
11 Titration of alanine ph=2.6 ph=10.0 H H 3 N C CH CH 3 H H 3 N C C - CH 3 H C C - CH
12 Titration of lysine H H 3 N C CH NH 3 ph=2.2 ph=9.0 ph=10.5 H H 3 N C C - NH 3 H C C - NH 3 H C C - NH
13 The Henderson-Hasselbalch equation HA H A - (1) K a K a = [H ][A - ]/[HA] (2) [H] = K a [HA]/[A - ] (3) - log[h ] = - logk a - log[ha]/[a - ] (4) ph = pk a log[a - ]/[HA] (5) ph = pk a log(r) (6) ph - pk a = log(r) (7) 10 (ph - pka) = R (8)
14 Acid and base fractions in a titration [A - ]/[HA] = R (1) [A - ] = [HA]R (2) We know that A T = [A - ] [HA] (3) Substitute eq. 2 in eq. 3 A T = [HA]R [HA] (4) = [HA](1 R) (5) [HA] = A T 1 (1 R) (6) Substitute rearranged eq. 2 in eq. 6 [A - ] = A T R (1 R) (7)
15 What is the charge of lysine at ph6.5? H H 3 N C C - NH 3 Lysine has 3 dissociable protons Calculate the charge of each one at a time
16 Start with the carboxyl group H H 3 N C C - NH 3 pka = (ph-pka) = R 10( ) = =20893 The dissociated C - carries a charge So use the equation for A - [A - ] = A T R/(1R) [A-] = /(120893) Charge = =
17 Next do the α-carbon amino pka = 8.95 H H 3 N C C - NH 3 10 (ph-pka) = R 10( ) = =0.004 The associated NH 3 carries a charge So use the equation for HA [HA] = A T /(1R) [HA] = 1 /( ) Charge = 0.996
18 Finally, do the side-chain amino H H 3 N C C - NH 3 pka = (ph-pka) = R 10( ) = = The associated NH 3 carries a charge So use the equation for HA [HA] = A T /(1R) [HA] = 1 /( ) Charge = 0.999
19 Add the charges from the different groups At ph6.5: Carboxyl: α-amino: Side-chain amino: Total charge = = 0.996
20 Programs exist the calculate the charge
21 Calculate the charge of the di-peptide EK at ph 7.0 The di-peptide EK pka = 9.47 H 3 N H pka = 2.18 C C N C C - H pka = 4.07 C - NH 3 pka = 10.5 A di-peptide has 4 dissociabale protons The charge at a given ph value can be calculated as demonstrated
22 Glutamic acid amino group 10 (ph-pka) = R 10( ) = = The associated NH 3 carries a charge So use the equation for HA [HA] = A T /(1R) [HA] = 1 /( ) Charge = 0.997
23 Glutamic acid carboxyl group 10 (ph-pka) = R 10( ) = = The dissociated C - carries a charge So use the equation for A - [A - ] = A T R/(1R) [A-] = /( ) Charge = =
24 Lysine amino group 10 (ph-pka) = R 10( ) = = The associated NH 3 carries a charge So use the equation for HA [HA] = A T /(1R) [HA] = 1 /( ) Charge = 0.999
25 Lysine carboxyl group 10 (ph-pka) = R 10( ) = =66, The dissociated C - carries a charge So use the equation for A - [A - ] = A T R/(1R) [A-] = 1. 66, /(1 66,069.34) Charge = =
26 Net charge =
27 Calculate the net charge of the tri-peptide DHR at ph 5.2 Amino acid C- NH3 Side-chain D H R Deadline Monday 6 Feb by 5pm BC334 mailbox at front door of Biotechnology Building Late submissions will not be marked No Excuses, No Exceptions
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
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
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
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
AMINO 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
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
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:
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
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
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
Guidelines 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
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 =
THE 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
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
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
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
Molecular 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
Peptide 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
Introduction 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,
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.
Amino 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
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
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
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)
Peptide 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
Journal 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
Application 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,
WORKING 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
Concluding 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:
UNIVERSITETET 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:.
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
Amino 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)
Protein 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
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)
Chapter 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
The 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
Amino 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
Application 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
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
Human 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
From 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
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
The 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
INFORMATIKA 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
Chapter 27: Amino Acids, Peptides, and Proteins. monomer unit: α-amino acids
Chapter 27: Amino Acids, Peptides, and Proteins. monomer unit: αamino acids 2 C 2! Amino Acid = sidechain Biopolymer: the monomeric amino acids are linked through an amide bond (the carboxylic acids of
Non-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
Acidic 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
systems 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,
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)
Chapter 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
Analysis 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
Pet 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
Amino 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
PMF IDENTIFICATION MS/MS VALIDATION
PMF IDENTIFICATION MS/MS VALIDATION rammentazione dei Peptidi x n-i v n-i y n-i z n-i y n-i-1 -HN-CH-CO-NH-CH-CO-NH- R i a i b i c i wn-i CH-R R i+1 i+1 b i+1 low energy fragmentation d i+1 high energy
Previously 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
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
Rapid and Reproducible Amino Acid Analysis of Physiological Fluids for Clinical Research Using LC/MS/MS with the atraq Kit
Rapid and Reproducible Amino Acid Analysis of Physiological Fluids for Clinical Research Using LC/MS/MS with the atraq Kit Fast, simple and cost effective analysis Many areas of biochemical research and
PEPTIDES, AND PROTEINS
A P T E AID, PEPTIDE, AD PTEI 24AMI Proteins are the most abundant organic molecules in animals, playing important roles in all aspects of cell structure and function. Proteins are biopolymers of 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
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
CHAPTER 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
Multiple 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.
Peptides & 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:
Covalent 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
AMINO 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:
Isoelectric point prediction from the amino acid sequence of a protein
Rochester Institute of Technology RIT Scholar Works Theses Thesis/Dissertation Collections Summer 2005 Isoelectric point prediction from the amino acid sequence of a protein Matthew Conte Follow this and
Previous 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
Bioinformatics, Sequences and Genomes
Bioinformatics, Sequences and Genomes BL4273 Bioinformatics for Biologists Week 1 Daniel Barker, School of Biology, University of St Andrews Email db60@st-andrews.ac.uk BL4273 and 4273π 4273π is a custom
How To Make A Monoclonal Antibody
MONOCLONAL ANTIBODIES AND ANTIBODY TECHNIQUES POLYCLONAL AND MONOCLONAL. When you work with antibodies, you will use either polyclonal antisera, or monoclonal antibodies. Polyclonal antisera are made in
Copyright 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
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
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
AMINO 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
Amino 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
General 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
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
PROTEINS 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
Insulin mrna to Protein Kit
Insulin mrna to Protein Kit A 3DMD Paper BioInformatics and Mini-Toober Folding Activity Teacher Key and Teacher Notes www. Insulin mrna to Protein Kit Contents Becoming Familiar with the Data... 3 Identifying
Peptide Synthesis. Technical Document. www.altabioscience.com. Why use AltaBioscience?
Peptide Synthesis Technical Document AltaBioscience offers a custom peptide synthesis service certified to ISO 9001:2008. With a strong focus on scientific excellence and 40 years of expertise we work
Evaluation of a LC-MS/MS method for quantitative amino acid analysis
Evaluation of a LC-MS/MS method for quantitative amino acid analysis Patrice K. Held, Ph.D. Assistant Professor of Pathology University of Utah School of Medicine Assistant Medical Director, Biochemical
Validation 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
Course Content. Amino Acids, Peptides & Proteins. Modules 06740 / 06741 / 06742
Amino Acids, Peptides & Proteins Modules 06740 / 06741 / 06742 1 Course Content 1. Introduction to amino acids and peptides 2. Separation and purification of amino acids and proteins 3. Chemical and enzymatic
Amino 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.
Separation and determination of the amino acids by ion exchange column chromatography applying postcolumn derivatization
Acta Univ. Sapientiae, Alimentaria, 1 (2008) 5 29 Separation and determination of the amino acids by ion exchange column chromatography applying postcolumn derivatization J. Csapó 1,2 email: csapo.janos@ke.hu
Acute 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.
Grow Taller 4 Idiots 2
1 Grow Taller 4 Idiots 2 Warning and Disclaimer Every effort has been made to make this digital book as complete and as accurate as possible, but no warranty or fitness is implied. The information provided
Preliminary 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
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
Hands on Simulation of Mutation
Hands on Simulation of Mutation Charlotte K. Omoto P.O. Box 644236 Washington State University Pullman, WA 99164-4236 omoto@wsu.edu ABSTRACT This exercise is a hands-on simulation of mutations and their
USP's Therapeutic Peptides Expert Panel discusses manufacturing processes and impurity control for synthetic peptide APIs.
Control Strategies for Synthetic Therapeutic Peptide APIs Part III: Manufacturing Process Considerations By Brian Gregg,Aleksander Swietlow,Anita Y. Szajek,Harold Rode,Michael Verlander,Ivo Eggen USP's
Part ONE. a. Assuming each of the four bases occurs with equal probability, how many bits of information does a nucleotide contain?
Networked Systems, COMPGZ01, 2012 Answer TWO questions from Part ONE on the answer booklet containing lined writing paper, and answer ALL questions in Part TWO on the multiple-choice question answer sheet.
(21) Appl. No.: 09/120,044
US 20010014332A1 (19) United States (12) Patent Application Publication (10) Pub. No.: US 2001/0014332 A1 MINETTI et al. (43) Pub. Date: Aug. 16, 2001 (54) MODIFIED IMMUNOGENIC PNEUMOLYSIN COMPOSITIONS
AMINO ACID ANALYSIS By High Performance Capillary Electrophoresis
AMINO ACID ANALYSIS By High Performance Capillary Electrophoresis Analysis of Amino Acid Standards Label free analysis using the HPCE-512 ABSTRACT Capillary electrophoresis using indirect UV detection
Protein. 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.
Refinement 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
Chapter 18. An Introduction to the Endocrine System. Hormone Chemistry
Chapter 18 An Introduction to the Endocrine System Hormone Chemistry Endocrine System Components endocrine system - glands, tissues, and cells that secrete hormones Copyright The McGraw-Hill Companies,
DETERMINATION OF AMINO ACID CONTENT IN ROMANIAN SALAMI BY ION-EXCHANGE CHROMATOGRAPHY
DETERMINATION OF AMINO ACID CONTENT IN ROMANIAN SALAMI BY ION-EXCHANGE CHROMATOGRAPHY Constantin BELE, Cristian MATEA, Andreea BUNEA, Carmen JECAN, Francisc DULF Abstract: Free amino acid content might
Transcription 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
Sidechain Torsional Potentials and Motion of Amino Acids in Proteins:
Proc. Nat. Acad. Sci. USA Vol. 72, No. 6, pp. 2002-2006, June 1975 Sidechain Torsional Potentials and Motion of Amino Acids in Proteins: Bovine Pancreatic Trypsin Inhibitor (nuclear magnetic resonance
Chemistry 201. Practical aspects of buffers. NC State University. Lecture 15
Chemistry 201 Lecture 15 Practical aspects of buffers NC State University The everyday ph scale To review what ph means in practice, we consider the ph of everyday substances that we know from experience.
FINAL REPORT. Submitted to: Mr. Arthur Hanks, Canadian Hemp Trade Alliance. Submitted by:
FINAL REPORT Evaluating the Quality of Protein from Hemp Seed and Hemp Seed Products Through the use of the Protein Digestibility- Corrected Amino Acid Score Method Submitted to: Mr. Arthur Hanks, Canadian