Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
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Chapter 2, Problem 12P
Interpretation Introduction
Interpretation:
The meaning of the term polypeptide backbone should be determined.
Concept introduction:
A peptide bond exists between the two amino acids. During the formation of a peptide bond, a molecule of water is released. The carboxyl group of one amino acid gets linked with the amino group of the other amino acid. Polypeptides and proteins are the chains formed by the amino acids.
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Figure 7 shows one additional type of bond that can stabilize the tertiary structure of a
protein. This bond is called a disulfide bond (or disulfide bridge), and it involves the
sulfhydryl (-SH) R groups from one particular type of amino acid. A disulfide bond can
form only under certain conditions (oxidative conditions). We'll talk about oxidation and
reduction next week. For now, just note that this type of bond does exist in some
proteins.
Answer the below questions on tertiary structure in your own document.
8. Figure 6 shows examples of bonds that might stabilize the tertiary structure of a
protein (labeled A, B, and C). Do these interactions involve only the amino acid R
groups, only the polypeptide backbone atoms, or both?
9. In the table below, indicate what type of bond/ interaction is represented in
the examples shown in Figure 6, panels A, B, and C and whether each
interaction involves group or backbone atoms.
Example
Type of Bonding Interaction
R group or backbone?
A
В
10.…
Protein Concept Map
Add these terms to your concept map should include these concepts and details:
Structure (functional groups, shape);
Monomer;
Linkage;
Properties;
Functions;
Key terms from the Partial List of Key Terms from the Minds
Partial List of Key Terms
essential amino acid
amino acid
side group/R-group
peptide bond
polypeptide
receptor
neurotransmitter
hormone
secondary structure
tertiary structure
quaternary structure
fair test
hydrophobic
hydrophilic
intermolecular force of attraction
Alpha-helix of proteins, its characteristics. Draw a diagram of the arrangement of amino acids in the alpha helix. Examples of proteins formed mainly by this structure.
Chapter 2 Solutions
Biochemistry
Ch. 2 - Prob. 1PCh. 2 - Prob. 2PCh. 2 - Prob. 3PCh. 2 - Prob. 4PCh. 2 - Prob. 5PCh. 2 - Prob. 6PCh. 2 - Prob. 7PCh. 2 - Prob. 8PCh. 2 - Prob. 9PCh. 2 - Prob. 10P
Ch. 2 - Prob. 11PCh. 2 - Prob. 12PCh. 2 - Prob. 13PCh. 2 - Prob. 14PCh. 2 - Prob. 15PCh. 2 - Prob. 16PCh. 2 - Prob. 17PCh. 2 - Prob. 18PCh. 2 - Prob. 19PCh. 2 - Prob. 20PCh. 2 - Prob. 21PCh. 2 - Prob. 22PCh. 2 - Prob. 23PCh. 2 - Prob. 24PCh. 2 - Prob. 25PCh. 2 - Prob. 26PCh. 2 - Prob. 27PCh. 2 - Prob. 28PCh. 2 - Prob. 29PCh. 2 - Prob. 30PCh. 2 - Prob. 31PCh. 2 - Prob. 32PCh. 2 - Prob. 33PCh. 2 - Prob. 34PCh. 2 - Prob. 35PCh. 2 - Prob. 36PCh. 2 - Prob. 37P
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- Below is the structure of glycine. Draw a tripeptide composed exclusively of glycine. Label the N-terminus and C-terminus. Draw a box around the peptide bonds.arrow_forwardDraw out the basic amino acid structure (not specific) What is a peptide bond?arrow_forwardMatch 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. secondaryarrow_forward
- Please draw a single polypeptide chain structure that has the following amino acids (leucine, alanine, cystine, argenine, glutomine, and leucine) as it would appear at physiological pH. Calculate the pl of the polypeptide. I will rate!arrow_forwardβ-pleated sheets and α-helices arise more from interactions in the peptide backbone than from the “R” groups of the individual monomers; they are examples of the (????) structure of a protein. Primary Tertiary Secondary Quaternary (????) are comprised of a nitrogenous base, a pentose sugar, and a phosphate group. Monosaccharides Amino acids Proteins Nucleotides (????) is the RNA transcript of the DNA sequence that determines the primary structure of a protein. mRNA lncRNA tRNA rRNA If a substance such as a lipid isn’t soluble in water it might be described as (????) Hydrophilic Hydrophobicarrow_forwardDoes your protein 3GRS have a quaternary structure??? talk about the tertiary structure of 3GRS. https://www.rcsb.org/arrow_forward
- Part I. Protein structure You have the toy model for a protein in the water (W) environment of the cell shown. a) How many residues (amino acids) does this toy protein have? b) How many hydrophobic (H), hydrophilic (P), and charged (C) residues are there? c) Sketch the molecule on your answer sheet and then show the positions of the favorable C-C (charge-charge) interactions on the figure.arrow_forwardPrepare & define the beta pleated structure of protein with examplesarrow_forwardTERTIARY STRUCTURE (A) (B) (C) Fg Eet Galand Sen 20e Figure 6. Examples of the arrangement of a-helices and B-sheets in folded protein domains. Copyright 2013 from Essential Cell Biology, 4th Edition by Alberts et al. Reproduced by permission of Garland Science/ Taylor & Francis LLC. Figure 6 shows three examples of how secondary structure elements can be arranged in relation to one another in the functional, folded form of a complete protein or one compact portion of a protein. The overall three-dimensional shape (or conformation) of a protein is its tertiary structure. • What do you think holds together the various secondary structural elements in a particular three-dimensional pattern? (Hint: Look back at Figure 5 - what is sticking out from the sides of the a-helices and B-strands?)arrow_forward
- Based on your understanding of the principles guiding folding of globular protein, briefly explain why a folded protein cannot consist of a single alpha-helix or single beta-strandarrow_forward7 Protein structure.Circle one of the three amino acid sequences that is most likely to form a stable a-helix? RASKTARQ DASKTAEQ KPGKPAGQ In one sentence (that can be accompanied by a small picture) explain why?arrow_forwarda) Canonical forces in protein folding. Describe how these forces come into play when a protein folds. Why do are other intermolecular interactions important to fully understand folding processes?arrow_forward
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