Amino acids are monomers from which proteins are constructed. Understanding the structure andcharacteris-tics of amino acids and the peptide bond that covalently links them to form peptides willaid in understanding larger, more complex protein structures. Proteins carry out a multitude of differentand important functions. The great variety in function is accomplished through a complex and variablepolymeric structure. Comprehending protein structure will give you a better understanding of how proteinscarry out their roles.WhyOutcomes1. Use the acid/base characteristics (pK, data) of the 20 amino acids found in proteins to determine thecharge of an amino acid at a given pH.2. Determine the pI of a small peptide.3. Identify the peptide bond and describe the structural features that characterize a peptide bond.4. Use information processing skills to draw conclusions about chemical characteristics of complexmolecules.Plan1. Form teams as instructed.2. The person whose hometown is the most distant from here assumes the role of team manager. The teammanager should assign remaining roles.3. Answer the Critical Thinking Questions.4. Prepare the spokesperson to articulate two discoveries the group has made that would help othersbetter process information in this chapter.Critical Thinking Questions1. Quickly review questions a through c below.a. What is the letter on the model titration curve of HPr that corresponds to the point where pHequals the numerical value of the pK, for HPr?b. Is the titration curve horizonal or vertical at this point that corresponds to pH pK,?c. What species of molecules are present at the point noted in question lb?

A titration curve is formed when the pH of sample solution changes with the addition of alkali or…

Critical Thinking Questions 1. Quickly review questions a through c below. a. What is the letter on the model titration curve of HPr that corresponds to the point where pH equals the numerical value of the pK, for HPr? b. Is the titration curve horizonal or vertical at this point that corresponds to pH = pK,? c. What species of molecules are present at the point noted in question 1b?

Critical Thinking Questions 1. Quickly review questions a through c below. a. What is the letter on the model titration curve of HPr that corresponds to the point where pH equals the numerical value of the pK, for HPr? b. Is the titration curve horizonal or vertical at this point that corresponds to pH = pK,? c. What species of molecules are present at the point noted in question 1b?

Biology (MindTap Course List)

11th Edition

ISBN:9781337392938

Author:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Publisher:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Chapter3: The Chemistry Of Life: Organic Compounds

Section: Chapter Questions

Problem 9TYU: Which of the following levels of protein structure may be affected by hydrogen bonding? (a) primary...

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Which of the following levels of protein structure may be affected by hydrogen bonding? (a) primary and secondary (b) primary and tertiary (c) secondary, tertiary, and quaternary (d) primary, secondary, and tertiary (e) primary, secondary, tertiary, and quaternary
Our growing understanding of how proteins fold allows researchers to make predictions about protein structure based on primary amino acid sequence data Consider the following amino acid sequence Ile-Ala-His-Thr-Tyr-Gly-Pro-Phe-Glu-Ala-Ala-Met-Cys-Lys-Trp-Glu-Ala-Gln-Pro-Asp-Gly-Met-Glu-Cys-Ala-Phe-His-Arg Where might reverse turns occur? Where might Intrachain disulfide linkages be formed? What will be the secondary structure formed from this sequence? Assuming that this sequence is part of a larger globular protein, indicate the probable location of the following amino acid residues: Asp, Ile, Thr, Ala. Gln, Lys.( Hint: see Hydropathy index)
ch one of the following statements about protein structure is NOT correct? . Domains are discrete parts of a protein structure, usually associated with a particula function. true Beta-sheets are stabilised by hydrogen bonds between amino-hydrogens and carbonyl-oxygens from peptide bonds. no adjacent hydrogen bonding Proteins made from three polypeptide chains show quaternary structure. Yes Smaller protein domains come together to from supersecondary structures and mo
Which of the following statements about protein structure is CORRECT O a. Fibrous proteins can have rigid quaternary structure O b. The stability of the quaternary structure in proteins is mainly a result of covalent bonds among the subunits O c. The denaturation of proteins always leads to irreversible loss of secondary and tertiary structure d. The information required for the correct folding of a protein is contained in the specific sequence of amino acids along the polypeptide chain O e. The formation of a disulfide bond in a protein requires that the two participating cysteine residues be adjacent to each other in the primary sequence of the protein
Match the following levels of protein structure with their description two or more polypeptide chains > > twisting and folding to form a 3-dimensional structure, dependent on the locations of the charged groups and polar groups within the amino acid chain, sometimes covalent bonds form between sulfur atoms (called disulfide bonds) alpha helix and beta- pleated sheets formed by the arrangement of hydrogen bonds between amino acids, many other shapes are possible amino acid sequence 1. quaternary 2. tertiary 3. primary 4. secondary
3. Amino Acid Sequence and Protein Structure Our growing understanding of how proteins fold allows researchers to make predictions about protein structure based on primary amino acid sequence data. Consider the following amino acid sequence. 1 3 5 6 7 8 9 10 Ile - Ala - His - Thr - Tyr - Gly - Pro - Phe-Glu – Ala- - 11 12 13 14 15 17 20 Ala - Mat - Cys- Lys - Trp - Glu-Ala-Gln-Pro - Asp- 16 18 19 21 22 23 24 25 26 27 28 Gly - Met-Glu - Cys - Ala - Phe - His - Arg (a) Where might bends or ß turns occur? (b) Where might intrachain disulfide cross-linkages be formed? (c) Assuming that this sequence is part of a larger globular protein, indicate the probable location (external surface or interior of the protein) of the following amino acid residues: Asp, lle, Thr, Ala, Gln, Lys. Explain your reasoning.
In the following diagram of a portion of a protein, label the types of interactions that are shown. What level of protein structure are these interactions producing? ____________________
Protein folding is critical for function because the properties of a protein arise from its overall shape and the distribution within that shape of the various amino acid side-chains. Which of the following statements about protein three-dimensional structure are correct? 1) the folding pattern of a protein is ultimately determined by its amino acid sequence. 2) proteins tend to fold in such a way that the hydrophobic amino acids are buried in the interior, while hydrophilic amino acids are exposed at the surface. 3) the chemical interactions within a protein molecule that support its overall folded structure are mostly covalent C-C (carbon to carbon) bonds between amino acid side-chains. 4) the overall folding pattern/shape of a protein molecule is termed its primary structure. 5) during evolution, the three-dimensional structure of a protein is often more strongly conserved than its amino acid sequence. More than one answer might be right
Tertiary structures refer to the three-dimensional arrangement of every atom in the molecule. On the other hand, primary structures refer to the stable arrangements of amino acid residues in a protein that give rise to recurring patterns. O Both statements are correct O Both statements are incorrect O The first statement is incorrect while the second statement is correct O The first statement is correct while the second statement is incorrect
When a protein folds into a quaternary structure the outside amino acids are exposed to the aqueous (water rich) environment. These amino acid R likely have what chemical properties? O The amino acid R groups are polar and hydrophilic The amino acid R groups are non-polar and hydrophobic O The amino acid R groups have hydrocarbon functional groups O The amino acid R groups have unreactive functional groups
Describe as completely as possible, the four levels of protein What type of bonds hold a protein together at the primary level? What type of bonds maintain the protein at the secondary and tertiary level? Give an example of secondary, tertiary, and quarternary level proteins. At which level is the protein functional? What happens (at a molecular level) when a protein is denatured?
Physical methods are often used to determine protein conformation. Describe how x-ray crystallography, cryo electron microscopy, and NMR spectroscopy can be used to determine the shapes of proteins. What are the advantages and disadvantages of each method? Which is better for small proteins? Large proteins? Huge macromolecular assemblies?