This exam consists of two parts. Part I is multiple choice. Each of these 25 questions is worth 2 points.
|
|
- Lora Stevens
- 5 years ago
- Views:
Transcription
1 MBB 407/511 Molecular Biology and Biochemistry First Examination - October 1, 2002 Name Social Security Number This exam consists of two parts. Part I is multiple choice. Each of these 25 questions is worth 2 points. Part II is short answer and drawing format. The first two of these questions are worth 15 pts each, and the last two are worth 10 pts each. Please write your answers to Part I here: Grade: Part I Part II II-1 II-2 II-3 II-4 Total 1
2 Part I. Multiple Choice. 1. The cellular process by which a DNA sequence is converted into a messenger RNA sequence is. (A) Reverse translation. (B) Transcription. (C) Reverse transcription. (D) Translation. 2. The principal function of the lysosome in eukaryotic cells is: (A) Protein synthesis. (B) Respiration. (C) Protein packaging. (D) Protein degradation. 3. The hydrophobic effect is primarily due to: (A) hydrogen-bonding between the hydrophobic group and water. (B) desolvation of hydrophobic groups in forming a "hydrophobic core", resulting in increased entropy of the system. (C) polar groups interacting in the "hydrophobic core". (D) all of the above. 4. For hydrogen bonds X-H --- Y, typical donor and acceptor atoms X and Y include: (A) O, N, or C (B) O, N, or S (C) C, N, or S (D) O, C, or S 5. A molecule which contains a hydrophilic head group and a hydrophobic tail is said to be: (A) polarized (B) amphipathic (C) orthorhombic (D) clathrate 6. It is well known that all of the common amino acids except glycine have chiral Cα atoms, and can be either L- or D-. One of the two common amino acids with a chiral Cβ atom in the side chain is: (A) Cysteine. (B) Serine. (C) Threonine. (D) Valine. 7. The ionization state of the cysteine sidechain at ph 10 is: (A) R-CH 2 -S-S-CH 2 -R' (B) R-CH 2 -SH (C) R-CH 2 -S - (D) R-CH 2 -S + 8. Given the following single strand of DNA: 5'-ATTGCACCT-3' the complementary stand of mrna which results from transcription is: (A) 3'-UAACGUGGA-5' (B) 3'-TUUCGTGGU-5' (C) 5'-UAACGUGGA-3' (D) 5'-TUUCGTGGU-3' 2
3 9. A-form RNA has a helical pitch of 2.8 nm / helical turn, and 11 residues per helical turn. Accordingly, the rise per residue ( Z / residue) is: (A) 2.55 nm. (B) 25.5 Å. (C) 2.55 Å (D) Å 10. The melanocyte-stimulating hormone α-melanotropin has the folowing sequence: Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-Gly-Lys-Pro-Val In the one-letter code of amino acids, this sequence would be: (A) STSMGHFAWGKPV (B) SYSMDHFAWGKPV (C) SYSMEHFAWGLPV (D) SYSMEHFRWGKPV 11. The right-handed α-helix is characterized by: (A) 3.6 Å / turn; 13 atoms per hydrogen-bonded loop. (B) 3.6 residues / turn; 13 atoms per hydrogen-bonded loop. (C) 3.6 residues / turn; 13 Å / turn. (D) 13 Å / turn; 3.6 atoms per hydrogen-bonded loop. 12. The helix-dipole moment can stabilize (or destabilize) the α- helical conformation by interacting with charged amino acids side chains at the N-terminal and C-terminal regions of the helical structure. Considering the distribution of charge which results from the helix dipole, would you expect: (A) positively charged amino acids at the C-terminus to destabilize the α-helix. (B) positively charged amino acids at the C-terminus to stabilize the α-helix. (C) negatively charged amino acids at the N-terminus to destabilize the α-helix. (D) negatively charged amino acids at the C-terminus to stabilize the α-helix. 13. In the absence of co-factors, hemes, and other prosthetic groups, the absorbtion spectra of proteins in the near UV range ( nm) are dominated by the amino acid: (A) Phenylalanine (B) Tyrosine (C) Tryptophan (D) Hisidine 3
4 14. The symmetry operator which maps the low energy regions of the Ramachandran plots for an L- amino acid (e.g. L-Ala) into the corresponding low energy region of the D- amino acid (e.g. D-Ala) is: (A) φ φ, ψ ψ. (B) φ φ, ψ ψ. (C) φ φ, ψ ψ. (D) φ φ, ψ ψ. 15. For the helix-to-coil transition in DNA, it is known that H hc > 0 and S hc > 0. From this it follows that: (A) G ch < 0 at low temperatures. (B) G ch < 0 at high temperatures. (C) G ch > 0 at low temperatures. (D) G hc > 0 at high temperatures 16. Consider a fully relaxed circle of 400 bp double-stranded circular DNA of linking number L = 40, twist T = 40 turns, and writhe W = 0. By the action of topoisomerase, this circle is supercoiled into a tertiary conformation of linking number L = 36, with twist T = 40 turns. The writhe of the resulting supercoil will be: (A) W = +4 (B) W = +2 (C) W = -2 (D) W = An amino acid with a hydrophilic side chain is: (A) Ile. (B) Leu. (C) Ala. (D) Asp. 18. For D-amino acids in synthetic polypeptides, most of the low energy regions of the Ramachandran plot have backbone dihedral angles: (A) psi > 0 (B) psi < 0. (C) phi > 0 (D) phi < Ion exchange chromatography is a method for separating macromolecules primarilly on the basis of their: (A) Size (B) Charge (C) Hydrophobicity (D) Salt content. 20. Consider a β-bend to be defined by the phi-phi residues at the 2nd and 3rd positions in the amino acid sequence. A type-ii β-bend requires a phi,psi value on the right side (phi > 0) of the Ramachandran diagram at position 3. This implies that a type-ii β-bend has a high probability for which type of amino acid commonly found in protein sequences at position 3: (A) Pro. (B) Gly. (C) Thr. (D) Ile 4
5 21. A pair of homologous proteins functioning in the same biological context in two different genomes (e.g. human and mouse myoglobin) are called: (A) Orthologs (B) Structural Genomics (C) Parallelogs (D) Divergalogs 22. Consider a small protein of 100 amino acids. Next, consider that the only degrees of freedom in this protein are the 100 phi angles, the 100 psi angles, and 50 sidechain chi-1 dihedral angles. Finally, consider that each of these 250 dihedral angles can adopt 10 (and only 10) independent values. What is the number of possible conformations for this small peptide? Assuming that it takes one nanosecond to sample each of these conformations, how long would it take to sample all possible conformations? (A) 250 conformations; 250 x 10-9 sec. (B) conformations; ~ 1 x sec (C) conformations; sec (D) 13!10!; (13!10!) x 10-9 sec. 23. Assuming that this 100 amino acid protein actually folds in about 1 millisec, estimate the size of a "folding domain" -- that is the number of dihedral angles in the effective "folding unit" (sometimes called "foldons"). (A) three dihedral angles (B) six dihedral angles. (C) twelve dihedral angles (D) twenty dihedral angles 24. Highest thermal stability is generally associated with DNA sequences containing: (A) High AT : GC ratios (B) Equal AT and GC content. (C) High GC : AT ratios. (D) High polya content. 25. The pk a is a characteristic of the equilibrium between an acid (HA) and its conjugate base (A - ). This relationship is given by: (A) pk a = - ln { [HA] / [H + ][A - ] } (B) pk a = - log { [HA] / [H + ][A - ] } (C) pk a = - ln { [H + ][A - ] / [HA] } (D) pk a = - log { [H + ][A - ] / [HA] } 5
6 Part II. Drawings and Derivations Question II-1.(15 pts) Draw the structure of the polypeptide: Phe-Pro-Asp-Ile in its ionization state at ph 7, showing any formal charges on each atom. Label on the structure the dihedral angles φ, ψ, ω, χ 1, and χ 2 of the amino acid residue Asp. 6
7 Question II-2 (15 pts) Draw the structure of the RNA oligonucleotide at ph 7 5'OH-AGC-PO 4-2 3' including the phosphate backbone (with correct charges indicated), the ribose ring, and the bases. For the adenine ribose ring, label the 1', 2', 3', 4', and 5' carbons. 7
8 Question II-3. (10 pts) A polypeptide sequence can be determined by cutting it into overlapping fragments with proteolytic enzymes, purifying these fragments by reversed-phase chromatography, and sequencing each of these peptides using an the Edman reaction. You have been given a 12 amino acid long polypeptide which plays an key role in tumor growth. Digestion of the peptide with the enzyme trypsin (which cuts after Arg and Lys residues) yields the following three peptides plus 1 equivalent of free arginine. Asp-Gln Leu-Ile-Phe-Ala-Lys Gly-Val-Tyr-Lys Subsequent digestion with chymotrypsin (which cuts after the aromatic residues Phe, Tyr, and Trp) yields the three peptides Lys-Arg-Leu-Ile-Phe Ala-Lys-Asp-Gln Gly-Val-Tyr Based on these data, determine the sequence of this peptide. 8
9 Question II-4. (10 pts). Design a sequence of polypeptide containing up to 25 amino acids which is likely to form a hairpin α-helical structure (two antiparallel α-helices), with a β-bend in the center of the sequence. Show you proposed sequence using the one-letter code of amino acids, and explain the special features of your design. In your sequence be sure to include the following features to favor α-helix formatation: (i) hydrophobic periodicity; (ii) charged sidechains oriented to interact favorably with the helical dipoles; (iii) good ionic interactions between the two α-helices Also include amino acids in the β-bend at the center of the sequence which favor β-bend formation. (Hint: Gly and Pro are both poor helix formers). 9
CS612 - Algorithms in Bioinformatics
Spring 2016 Protein Structure February 7, 2016 Introduction to Protein Structure A protein is a linear chain of organic molecular building blocks called amino acids. Introduction to Protein Structure Amine
More informationMolecular Biology. general transfer: occurs normally in cells. special transfer: occurs only in the laboratory in specific conditions.
Chapter 9: Proteins Molecular Biology replication general transfer: occurs normally in cells transcription special transfer: occurs only in the laboratory in specific conditions translation unknown transfer:
More informationAmino Acids. Review I: Protein Structure. Amino Acids: Structures. Amino Acids (contd.) Rajan Munshi
Review I: Protein Structure Rajan Munshi BBSI @ Pitt 2005 Department of Computational Biology University of Pittsburgh School of Medicine May 24, 2005 Amino Acids Building blocks of proteins 20 amino acids
More informationObjective: You will be able to explain how the subcomponents of
Objective: You will be able to explain how the subcomponents of nucleic acids determine the properties of that polymer. Do Now: Read the first two paragraphs from enduring understanding 4.A Essential knowledge:
More informationBiological systems interact, and these systems and their interactions possess complex properties. STOP at enduring understanding 4A
Biological systems interact, and these systems and their interactions possess complex properties. STOP at enduring understanding 4A Homework Watch the Bozeman video called, Biological Molecules Objective:
More informationProperties of amino acids in proteins
Properties of amino acids in proteins one of the primary roles of DNA (but far from the only one!!!) is to code for proteins A typical bacterium builds thousands types of proteins, all from ~20 amino acids
More informationReview II: The Molecules of Life
Review II: The Molecules of Life Judy Wieber BBSI @ Pitt 2007 Department of Computational Biology University of Pittsburgh School of Medicine May 24, 2007 Outline Introduction Proteins Carbohydrates Lipids
More informationChemical Nature of the Amino Acids. Table of a-amino Acids Found in Proteins
Chemical Nature of the Amino Acids All peptides and polypeptides are polymers of alpha-amino acids. There are 20 a- amino acids that are relevant to the make-up of mammalian proteins (see below). Several
More informationProteins are sometimes only produced in one cell type or cell compartment (brain has 15,000 expressed proteins, gut has 2,000).
Lecture 2: Principles of Protein Structure: Amino Acids Why study proteins? Proteins underpin every aspect of biological activity and therefore are targets for drug design and medicinal therapy, and in
More informationThe Basics: A general review of molecular biology:
The Basics: A general review of molecular biology: DNA Transcription RNA Translation Proteins DNA (deoxy-ribonucleic acid) is the genetic material It is an informational super polymer -think of it as the
More information2. Which of the following amino acids is most likely to be found on the outer surface of a properly folded protein?
Name: WHITE Student Number: Answer the following questions on the computer scoring sheet. 1 mark each 1. Which of the following amino acids would have the highest relative mobility R f in normal thin layer
More informationBiomolecules: amino acids
Biomolecules: amino acids Amino acids Amino acids are the building blocks of proteins They are also part of hormones, neurotransmitters and metabolic intermediates There are 20 different amino acids in
More informationBioinformatics for molecular biology
Bioinformatics for molecular biology Structural bioinformatics tools, predictors, and 3D modeling Structural Biology Review Dr Research Scientist Department of Microbiology, Oslo University Hospital -
More informationIntroduction to Protein Structure Collection
Introduction to Protein Structure Collection Teaching Points This collection is designed to introduce students to the concepts of protein structure and biochemistry. Different activities guide students
More informationShort polymer. Dehydration removes a water molecule, forming a new bond. Longer polymer (a) Dehydration reaction in the synthesis of a polymer
HO 1 2 3 H HO H Short polymer Dehydration removes a water molecule, forming a new bond Unlinked monomer H 2 O HO 1 2 3 4 H Longer polymer (a) Dehydration reaction in the synthesis of a polymer HO 1 2 3
More informationBiochemistry - I. Prof. S. Dasgupta Department of Chemistry Indian Institute of Technology, Kharagpur Lecture 1 Amino Acids I
Biochemistry - I Prof. S. Dasgupta Department of Chemistry Indian Institute of Technology, Kharagpur Lecture 1 Amino Acids I Hello, welcome to the course Biochemistry 1 conducted by me Dr. S Dasgupta,
More informationCopyright 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings
Concept 5.4: Proteins have many structures, resulting in a wide range of functions Proteins account for more than 50% of the dry mass of most cells Protein functions include structural support, storage,
More informationChapter 3: Amino Acids and Peptides
Chapter 3: Amino Acids and Peptides BINF 6101/8101, Spring 2018 Outline 1. Overall amino acid structure 2. Amino acid stereochemistry 3. Amino acid sidechain structure & classification 4. Non-standard
More informationJudy Wieber. Department of Computational Biology. May 27, 2008
Review II: The Molecules of Life Judy Wieber BBSI @ Pitt 2008 Department of Computational Biology University it of Pittsburgh School of Medicine i May 27, 2008 Outline Introduction Proteins Carbohydrates
More informationIntroduction to proteins and protein structure
Introduction to proteins and protein structure The questions and answers below constitute an introduction to the fundamental principles of protein structure. They are all available at [link]. What are
More informationMultiple-Choice Questions Answer ALL 20 multiple-choice questions on the Scantron Card in PENCIL
Multiple-Choice Questions Answer ALL 20 multiple-choice questions on the Scantron Card in PENCIL For Questions 1-10 choose ONE INCORRECT answer. 1. Which ONE of the following statements concerning the
More informationPractice Problems 3. a. What is the name of the bond formed between two amino acids? Are these bonds free to rotate?
Life Sciences 1a Practice Problems 3 1. Draw the oligopeptide for Ala-Phe-Gly-Thr-Asp. You do not need to indicate the stereochemistry of the sidechains. Denote with arrows the bonds formed between the
More informationLipids: diverse group of hydrophobic molecules
Lipids: diverse group of hydrophobic molecules Lipids only macromolecules that do not form polymers li3le or no affinity for water hydrophobic consist mostly of hydrocarbons nonpolar covalent bonds fats
More informationThe Structure and Function of Macromolecules
The Structure and Function of Macromolecules Macromolecules are polymers Polymer long molecule consisting of many similar building blocks. Monomer the small building block molecules. Carbohydrates, proteins
More informationFour Classes of Biological Macromolecules. Biological Macromolecules. Lipids
Biological Macromolecules Much larger than other par4cles found in cells Made up of smaller subunits Found in all cells Great diversity of func4ons Four Classes of Biological Macromolecules Lipids Polysaccharides
More informationMethionine (Met or M)
Fig. 5-17 Nonpolar Fig. 5-17a Nonpolar 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) Polar Trypotphan (Trp
More informationMacromolecules of Life -3 Amino Acids & Proteins
Macromolecules of Life -3 Amino Acids & Proteins Shu-Ping Lin, Ph.D. Institute of Biomedical Engineering E-mail: splin@dragon.nchu.edu.tw Website: http://web.nchu.edu.tw/pweb/users/splin/ Amino Acids Proteins
More informationMoorpark College Chemistry 11 Fall Instructor: Professor Gopal. Examination # 5: Section Five May 7, Name: (print)
Moorpark College Chemistry 11 Fall 2013 Instructor: Professor Gopal Examination # 5: Section Five May 7, 2013 Name: (print) Directions: Make sure your examination contains TEN total pages (including this
More informationMidterm 1 Last, First
Midterm 1 BIS 105 Prof. T. Murphy April 23, 2014 There should be 6 pages in this exam. Exam instructions (1) Please write your name on the top of every page of the exam (2) Show all work for full credit
More informationGentilucci, Amino Acids, Peptides, and Proteins. Peptides and proteins are polymers of amino acids linked together by amide bonds CH 3
Amino Acids Peptides and proteins are polymers of amino acids linked together by amide bonds Aliphatic Side-Chain Amino Acids - - H CH glycine alanine 3 proline valine CH CH 3 - leucine - isoleucine CH
More information9/6/2011. Amino Acids. C α. Nonpolar, aliphatic R groups
Amino Acids Side chains (R groups) vary in: size shape charge hydrogen-bonding capacity hydrophobic character chemical reactivity C α Nonpolar, aliphatic R groups Glycine (Gly, G) Alanine (Ala, A) Valine
More informationpaper and beads don t fall off. Then, place the beads in the following order on the pipe cleaner:
Beady Pipe Cleaner Proteins Background: Proteins are the molecules that carry out most of the cell s dayto-day functions. While the DNA in the nucleus is "the boss" and controls the activities of the cell,
More informationReactions and amino acids structure & properties
Lecture 2: Reactions and amino acids structure & properties Dr. Sameh Sarray Hlaoui Common Functional Groups Common Biochemical Reactions AH + B A + BH Oxidation-Reduction A-H + B-OH + energy ª A-B + H
More informationLAB#23: Biochemical Evidence of Evolution Name: Period Date :
LAB#23: Biochemical Evidence of Name: Period Date : Laboratory Experience #23 Bridge Worth 80 Lab Minutes If two organisms have similar portions of DNA (genes), these organisms will probably make similar
More information1. Describe the relationship of dietary protein and the health of major body systems.
Food Explorations Lab I: The Building Blocks STUDENT LAB INVESTIGATIONS Name: Lab Overview In this investigation, you will be constructing animal and plant proteins using beads to represent the amino acids.
More informationBiology. Lectures winter term st year of Pharmacy study
Biology Lectures winter term 2008 1 st year of Pharmacy study 3 rd Lecture Chemical composition of living matter chemical basis of life. Atoms, molecules, organic compounds carbohydrates, lipids, proteins,
More informationThe Structure and Function of Large Biological Molecules Part 4: Proteins Chapter 5
Key Concepts: The Structure and Function of Large Biological Molecules Part 4: Proteins Chapter 5 Proteins include a diversity of structures, resulting in a wide range of functions Proteins Enzymatic s
More informationLevels of Protein Structure:
Levels of Protein Structure: PRIMARY STRUCTURE (1 ) - Defined, non-random sequence of amino acids along the peptide backbone o Described in two ways: Amino acid composition Amino acid sequence M-L-D-G-C-G
More informationCHAPTER 21: Amino Acids, Proteins, & Enzymes. General, Organic, & Biological Chemistry Janice Gorzynski Smith
CHAPTER 21: Amino Acids, Proteins, & Enzymes General, Organic, & Biological Chemistry Janice Gorzynski Smith CHAPTER 21: Amino Acids, Proteins, Enzymes Learning Objectives: q The 20 common, naturally occurring
More informationPage 8/6: The cell. Where to start: Proteins (control a cell) (start/end products)
Page 8/6: The cell Where to start: Proteins (control a cell) (start/end products) Page 11/10: Structural hierarchy Proteins Phenotype of organism 3 Dimensional structure Function by interaction THE PROTEIN
More informationAP Bio. Protiens Chapter 5 1
Concept.4: Proteins have many structures, resulting in a wide range of functions Proteins account for more than 0% of the dry mass of most cells Protein functions include structural support, storage, transport,
More informationChemistry 121 Winter 17
Chemistry 121 Winter 17 Introduction to Organic Chemistry and Biochemistry Instructor Dr. Upali Siriwardane (Ph.D. Ohio State) E-mail: upali@latech.edu Office: 311 Carson Taylor Hall ; Phone: 318-257-4941;
More informationChapter 5: Structure and Function of Macromolecules AP Biology 2011
Chapter 5: Structure and Function of Macromolecules AP Biology 2011 1 Macromolecules Fig. 5.1 Carbohydrates Lipids Proteins Nucleic Acids Polymer - large molecule consisting of many similar building blocks
More informationCHM333 LECTURE 6: 1/25/12 SPRING 2012 Professor Christine Hrycyna AMINO ACIDS II: CLASSIFICATION AND CHEMICAL CHARACTERISTICS OF EACH AMINO ACID:
AMINO ACIDS II: CLASSIFICATION AND CHEMICAL CHARACTERISTICS OF EACH AMINO ACID: - The R group side chains on amino acids are VERY important. o Determine the properties of the amino acid itself o Determine
More informationPROTEINS. Building blocks, structure and function. Aim: You will have a clear picture of protein construction and their general properties
PROTEINS Building blocks, structure and function Aim: You will have a clear picture of protein construction and their general properties Reading materials: Compendium in Biochemistry, page 13-49. Microbiology,
More informationPROTEINS. Amino acids are the building blocks of proteins. Acid L-form * * Lecture 6 Macromolecules #2 O = N -C -C-O.
Proteins: Linear polymers of amino acids workhorses of the cell tools, machines & scaffolds Lecture 6 Macromolecules #2 PRTEINS 1 Enzymes catalysts that mediate reactions, increase reaction rate Structural
More informationProtein Secondary Structure
Protein Secondary Structure Reading: Berg, Tymoczko & Stryer, 6th ed., Chapter 2, pp. 37-45 Problems in textbook: chapter 2, pp. 63-64, #1,5,9 Directory of Jmol structures of proteins: http://www.biochem.arizona.edu/classes/bioc462/462a/jmol/routines/routines.html
More informationAmino Acids. Amino Acids. Fundamentals. While their name implies that amino acids are compounds that contain an NH. 3 and CO NH 3
Fundamentals While their name implies that amino acids are compounds that contain an 2 group and a 2 group, these groups are actually present as 3 and 2 respectively. They are classified as α, β, γ, etc..
More informationCells. Variation and Function of Cells
Cells Variation and Function of Cells Plasma Membrane= the skin of a cell, it protects and nourishes the cell while communicating with other cells at the same time. Lipid means fat and they are hydrophobic
More information(65 pts.) 27. (10 pts.) 28. (15 pts.) 29. (10 pts.) TOTAL (100 points) Moorpark College Chemistry 11 Spring Instructor: Professor Gopal
Moorpark College Chemistry 11 Spring 2012 Instructor: Professor Gopal Examination # 5: Section Five May 1, 2012 Name: (print) GOOD LUCK! Directions: Make sure your examination contains TWELVE total pages
More informationThe three important structural features of proteins:
The three important structural features of proteins: a. Primary (1 o ) The amino acid sequence (coded by genes) b. Secondary (2 o ) The interaction of amino acids that are close together or far apart in
More informationOrganic molecules are molecules that contain carbon and hydrogen.
Organic Chemistry, Biochemistry Introduction Organic molecules are molecules that contain carbon and hydrogen. All living things contain these organic molecules: carbohydrates, lipids, proteins, and nucleic
More informationFor questions 1-4, match the carbohydrate with its size/functional group name:
Chemistry 11 Fall 2013 Examination #5 PRACTICE 1 ANSWERS For the first portion of this exam, select the best answer choice for the questions below and mark the answers on your scantron. Then answer the
More informationBiomolecules Amino Acids & Protein Chemistry
Biochemistry Department Date: 17/9/ 2017 Biomolecules Amino Acids & Protein Chemistry Prof.Dr./ FAYDA Elazazy Professor of Biochemistry and Molecular Biology Intended Learning Outcomes ILOs By the end
More information(30 pts.) 16. (24 pts.) 17. (20 pts.) 18. (16 pts.) 19. (5 pts.) 20. (5 pts.) TOTAL (100 points)
Moorpark College Chemistry 11 Spring 2009 Instructor: Professor Torres Examination # 5: Section Five April 30, 2009 ame: (print) ame: (sign) Directions: Make sure your examination contains TWELVE total
More informationFor questions 1-4, match the carbohydrate with its size/functional group name:
Chemistry 11 Fall 2013 Examination #5 PRACTICE 1 For the first portion of this exam, select the best answer choice for the questions below and mark the answers on your scantron. Then answer the free response
More informationQ1: Circle the best correct answer: (15 marks)
Q1: Circle the best correct answer: (15 marks) 1. Which one of the following incorrectly pairs an amino acid with a valid chemical characteristic a. Glycine, is chiral b. Tyrosine and tryptophan; at neutral
More informationAmino Acids. Lecture 4: Margaret A. Daugherty. Fall Swiss-prot database: How many proteins? From where?
Lecture 4: Amino Acids Margaret A. Daugherty Fall 2004 Swiss-prot database: How many proteins? From where? 1986 Use http://us.expasy.org to get to swiss-prot database Proteins are the workhorses of the
More informationMacromolecules Structure and Function
Macromolecules Structure and Function Within cells, small organic molecules (monomers) are joined together to form larger molecules (polymers). Macromolecules are large molecules composed of thousands
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 information1. (38 pts.) 2. (25 pts.) 3. (15 pts.) 4. (12 pts.) 5. (10 pts.) Bonus (12 pts.) TOTAL (100 points)
Moorpark College Chemistry 11 Spring 2010 Instructor: Professor Torres Examination #5: Section Five May 4, 2010 ame: (print) ame: (sign) Directions: Make sure your examination contains TWELVE total pages
More informationHead. Tail. Carboxyl group. group. group. air water. Hydrocarbon chain. lecture 5-sa Seth Copen Goldstein 2.
Lipids Some lipid structures Organic compounds Amphipathic Polar head group (hydrophilic) Non-polar tails (hydrophobic) Lots of uses Energy storage Membranes Hormones Vitamins HO O C H 2 C CH 2 H 2 C CH
More informationMoorpark College Chemistry 11 Fall Instructor: Professor Gopal. Examination #5: Section Five December 7, Name: (print) Section:
Moorpark College Chemistry 11 Fall 2011 Instructor: Professor Gopal Examination #5: Section Five December 7, 2011 Name: (print) Section: alkene < alkyne < amine < alcohol < ketone < aldehyde < amide
More informationAA s are the building blocks of proteins
Chamras Chemistry 106 Lecture otes Chapter 24: Amino Acids, Peptides, and Proteins General Formula: () n (') α-amino Acids: (n = 1) Example: Amino Acids and Proteins: Glycine Alanine Valine AA s are the
More informationBIRKBECK COLLEGE (University of London)
BIRKBECK COLLEGE (University of London) SCHOOL OF BIOLOGICAL SCIENCES M.Sc. EXAMINATION FOR INTERNAL STUDENTS ON: Postgraduate Certificate in Principles of Protein Structure MSc Structural Molecular Biology
More information1-To know what is protein 2-To identify Types of protein 3- To Know amino acids 4- To be differentiate between essential and nonessential amino acids
Amino acids 1-To know what is protein 2-To identify Types of protein 3- To Know amino acids 4- To be differentiate between essential and nonessential amino acids 5-To understand amino acids synthesis Amino
More informationClassification of amino acids: -
Page 1 of 8 P roteinogenic amino acids, also known as standard, normal or primary amino acids are 20 amino acids that are incorporated in proteins and that are coded in the standard genetic code (subunit
More informationA Chemical Look at Proteins: Workhorses of the Cell
A Chemical Look at Proteins: Workhorses of the Cell A A Life ciences 1a Lecture otes et 4 pring 2006 Prof. Daniel Kahne Life requires chemistry 2 amino acid monomer and it is proteins that make the chemistry
More informationWater. High Boiling Point
High Boiling Point Water High Specific Heat (Heat Capacity) Very polar universal solvent Density solid < Density of Liquid Each H 2 O can make 4 H-bonds Permanent Dipole (b/c of shape and bond angles)
More informationProtein Structure Klemens Wild, BZH,
Protein Structure recommended books Proteins protein definition From gr. proteios (superior, erstrangig) 1836 JJ Berzelius Functions: structural, enzymes, muscle, transport immune system, Linear polymer
More informationBIOCHEMISTRY 460 FIRST HOUR EXAMINATION FORM A (yellow) ANSWER KEY February 11, 2008
WRITE YOUR AND I.D. NUMBER LEGIBLY ON EVERY PAGE PAGES WILL BE SEPARATED FOR GRADING! CHECK TO BE SURE YOU HAVE 6 PAGES, (print): ANSWERS INCLUDING COVER PAGE. I swear/affirm that I have neither given
More information9/16/15. Properties of Water. Benefits of Water. More properties of water
Properties of Water Solid/Liquid Density Water is densest at 4⁰C Ice floats Allows life under the ice Hydrogen bond Ice Hydrogen bonds are stable Liquid water Hydrogen bonds break and re-form Benefits
More informationLecture 4: 8/26. CHAPTER 4 Protein Three Dimensional Structure
Lecture 4: 8/26 CHAPTER 4 Protein Three Dimensional Structure Summary of the Lecture 3 There are 20 amino acids and only the L isomer amino acid exist in proteins Each amino acid consists of a central
More informationBio Factsheet. Proteins and Proteomics. Number 340
Number 340 Proteins and Proteomics Every living thing on the planet is composed of cells, and cells in turn are made of many types of molecules, including the biological molecules carbohydrates, lipids,
More informationBIO 311C Spring Lecture 15 Friday 26 Feb. 1
BIO 311C Spring 2010 Lecture 15 Friday 26 Feb. 1 Illustration of a Polypeptide amino acids peptide bonds Review Polypeptide (chain) See textbook, Fig 5.21, p. 82 for a more clear illustration Folding and
More informationActivities for the α-helix / β-sheet Construction Kit
Activities for the α-helix / β-sheet Construction Kit The primary sequence of a protein, composed of amino acids, determines the organization of the sequence into the secondary structure. There are two
More informationChem Lecture 2 Protein Structure
Chem 452 - Lecture 2 Protein Structure 110923 Proteins are the workhorses of a living cell and involve themselves in nearly all of the activities that take place in a cell. Their wide range of structures
More informationAmino acids. Side chain. -Carbon atom. Carboxyl group. Amino group
PROTEINS Amino acids Side chain -Carbon atom Amino group Carboxyl group Amino acids Primary structure Amino acid monomers Peptide bond Peptide bond Amino group Carboxyl group Peptide bond N-terminal (
More informationProtein structure. Dr. Mamoun Ahram Summer semester,
Protein structure Dr. Mamoun Ahram Summer semester, 2017-2018 Overview of proteins Proteins have different structures and some have repeating inner structures, other do not. A protein may have gazillion
More informationProtein Structure Monday, March
Michael Morales ffice: 204/202 ary; knock hard if you visit as my office is some door. Lab: 238 & 205 ary ffice hours Either make an appointment or just drop by Phone: 829-3965 E-Mail: moralesm@buffalo.edu
More informationPHAR3316 Pharmacy biochemistry Exam #2 Fall 2010 KEY
1. How many protons is(are) lost when the amino acid Asparagine is titrated from its fully protonated state to a fully deprotonated state? A. 0 B. 1 * C. 2 D. 3 E. none Correct Answer: C (this question
More informationIntroduction. Basic Structural Principles PDB
BCHS 6229 Protein Structure and Function Lecture 1 (October 11, 2011) Introduction Basic Structural Principles PDB 1 Overview Main Goals: Carry out a rapid review of the essentials of protein structure
More informationAmino acids & Protein Structure Chemwiki: Chapter , with most emphasis on 16.3, 16.4 and 16.6
Amino acids & Protein Structure Chemwiki: Chapter 16. 16.1, 16.3-16.9 with most emphasis on 16.3, 16.4 and 16.6 1 1. Most jobs (except information storage) in cells are performed by proteins. 2. Proteins
More informationReading from the NCBI
Reading from the NCBI http://www.ncbi.nlm.nih.gov/books/bv.fcgi?highlight=thermodyn amics&rid=stryer.section.156#167 http://www.ncbi.nlm.nih.gov/books/bv.fcgi?highlight=stability,pr otein&rid=stryer.section.365#371
More informationTowards a New Paradigm in Scientific Notation Patterns of Periodicity among Proteinogenic Amino Acids [Abridged Version]
Earth/matriX: SCIENCE TODAY Towards a New Paradigm in Scientific Notation Patterns of Periodicity among Proteinogenic Amino Acids [Abridged Version] By Charles William Johnson Earth/matriX Editions P.O.
More information!"#$%&' (#%) /&'(2+"( /&3&4,, ! " #$% - &'()!% *-sheet -(!-Helix - &'(&') +,(-. - &'()&+) /&%.(0&+(! - &'(1&2%( Basic amino acids
Basic amino acids pk ~ 10.5 pk ~ 12.5 pk ~ 6.0 Polar 25!"#$%&' (#%)! " #$% - &'()!% *-sheet -(!-Helix - &'(&') +,(-. - &'()&+) /&%.(0&+(! - &'(1&2%( /&'(2+"( /&3&4,, :++55 ('&.! 6($.(" 40 > 3&4,, ('&.!
More informationLecture 10 More about proteins
Lecture 10 More about proteins Today we're going to extend our discussion of protein structure. This may seem far-removed from gene cloning, but it is the path to understanding the genes that we are cloning.
More informationCells N5 Homework book
1 Cells N5 Homework book 2 Homework 1 3 4 5 Homework2 Cell Ultrastructure and Membrane 1. Name and give the function of the numbered organelles in the cell below: A E B D C 2. Name 3 structures you might
More informationSecondary Structure. by hydrogen bonds
Secondary Structure In the previous protein folding activity, you created a hypothetical 15-amino acid protein and learned that basic principles of chemistry determine how each protein spontaneously folds
More informationPAPER No. : 16, Bioorganic and biophysical chemistry MODULE No. : 22, Mechanism of enzyme catalyst reaction (I) Chymotrypsin
Subject Paper No and Title 16 Bio-organic and Biophysical Module No and Title 22 Mechanism of Enzyme Catalyzed reactions I Module Tag CHE_P16_M22 Chymotrypsin TABLE OF CONTENTS 1. Learning outcomes 2.
More informationRaghad Abu Jebbeh. Amani Nofal. Mamoon Ahram
... 14 Raghad Abu Jebbeh Amani Nofal Mamoon Ahram This sheet includes part of lec.13 + lec.14. Amino acid peptide protein Terminology: 1- Residue: a subunit that is a part of a large molecule. 2- Dipeptide:
More informationSupplementary Figure-1. SDS PAGE analysis of purified designed carbonic anhydrase enzymes. M1-M4 shown in lanes 1-4, respectively, with molecular
Supplementary Figure-1. SDS PAGE analysis of purified designed carbonic anhydrase enzymes. M1-M4 shown in lanes 1-4, respectively, with molecular weight markers (M). Supplementary Figure-2. Overlay of
More informationFour melanocyte-stimulating hormones have the following amino acid sequences:
Assignment 14: Melanocyte-stimulating hormone belongs to a group called the melanocortins. This group includes ACTH, alpha-msh, beta-msh and gamma-msh; these peptides are all cleavage products of a large
More informationMBB 694:407, 115:511. Please use BLOCK CAPITAL letters like this --- A, B, C, D, E. Not lowercase!
MBB 694:407, 115:511 First Test Severinov/Deis Tue. Sep. 30, 2003 Name Index number (not SSN) Row Letter Seat Number This exam consists of two parts. Part I is multiple choice. Each of these 25 questions
More informationIf you like us, please share us on social media. The latest UCD Hyperlibrary newsletter is now complete, check it out.
Sign In Forgot Password Register username username password password Sign In If you like us, please share us on social media. The latest UCD Hyperlibrary newsletter is now complete, check it out. ChemWiki
More information7.012 F 04 Problem Set 1 September 10 th 2004
MIT Biology Department 7.012: Introductory Biology Fall 2004 Instructors: Professor Eric Lander, Professor Robert A. Weinberg, Dr. laudette Gardel ame Question 1 TA Section 7.012 F 04 Problem Set 1 September
More informationDraw how two amino acids form the peptide bond. Draw in the space below:
Name Date Period Modeling Protein Folding Draw how two amino acids form the peptide bond. Draw in the space below: What we are doing today: The core idea in life sciences is that there is a fundamental
More informationAMINO ACIDS STRUCTURE, CLASSIFICATION, PROPERTIES. PRIMARY STRUCTURE OF PROTEINS
AMINO ACIDS STRUCTURE, CLASSIFICATION, PROPERTIES. PRIMARY STRUCTURE OF PROTEINS Elena Rivneac PhD, Associate Professor Department of Biochemistry and Clinical Biochemistry State University of Medicine
More information