Which is an appropriate statement of involvement of the hydrophobic effect inprotein folding?A) Nonpolar portions interact with polar portions in the interior of the protein.OB) Nonpolar portions of the molecule associate with one another in the interiorof the protein.OC) Nonpolar portions of the molecule can be placed on the surface of themolecule only if hydrogen bonded to water.OD) Polar portions of the molecule are generally exposed to solvent to interacteffectively with water.

Proteins are composed of amino acids, which are bound together by peptide linkage. Amino acids…

Answered: Which is an appropriate statement of…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Protein structure and function: a) Name two common post-translational modifications of proteins in the cell that will affect their structure/function. b) What are prions? Briefly describe their structure and function. C) Explain the principles of protein folding and significance of urea and Bmercaptoethanol in the experimental procedures addressing this question.
Consider the synthesis of a polypeptide by a ribosome of a prokaryote cell. As the polymerization of amino acids to form a polypeptide chain occurs and the molecule is still completely linear, what is the level of structure in the protein? a) primary, b) secondary, c) tertiary, d) quaternary, e) Because they are ionic, they only form crystals.
7) The figure below shows a 3-barrel protein embedded in a hydrophobic membrane. The central cavity of the B-barrel protein is open to aqueous solvent. Which of the following sequences belongs to one of B-strands that forms part of the B-barrel protein? A) LVMIAVL B) ETSDGHR C) LVIMDRE hydrophobic membrane D) VQLTAKL A hydrophoble membrane water-filled cavity
Currently, aspartic acid is forming an ionic interaction with arginine in a protein. Part a) If arginine is replaced with glutamic acid, would the ionic interaction have its stability increased, decreased, or have no effect on the ionic interaction? Part b) If arginine is replaced with Lysine, would the ionic interaction have its stability increased, decreased, or have no effect on the ionic interaction? Part c) If arginine is replaced with isoleucine, would the ionic interaction have its stability increased, decreased, or have no effect on the ionic interaction?
If Kd= 100 nM, [RNA] = 10 nM, and [protein] = 1 uM a) What fraction of RNA is bound? b) What fraction of protein is bound? c) What is the concentration of the protein:RNA complex? d) Is it reasonable to assume that total protein = free protein? e) Is it reasonable to assume that total RNA = free RNA?
For the three peptides below, label whether they would form an amphiphilic beta-strand, amphiphilic helix, or nothing. Explain why. Part a) S-V-K-I-Q-M-R-A-D-L Part b) A-L-E-H-M-F-R-Y-L-A-K Part c) A-L-A-I-W-F-P-D-R-K-E
Which of the following (could be more than one) would not be a rational explanation for why the three-dimensional structure of a protein is driven and stabilized largely by noncovalent rather than covalent bonds?a) Proteins may be degraded for energy, and if their three-dimensional structures were heldtogether by mostly covalent bonding, this might be too difficult to accomplishb) Proteins will need to be unfolded to cross biological membrane, and if their three-dimensionalstructures were held together by mostly covalent bonding, this might be too difficult toaccomplish.c) Protein function (transport, enzyme catalysis, etc...) may require flexibility in the three-dimensional structure to allow for conformational change, and if protein three-dimensionalstructure were held together by mostly covalent bonding, this might be too difficult toaccomplish.d) All of the answer choices are rational explanations for why the three-dimensional structure of protein is driven and stabilized largely…
Consider the synthesis of a polypeptide by a prokaryote ribosome. When the polymerization of amino acids to form a polypeptide chain occurs and the molecule is still completely linear, what is the level of structure in the protein? A) primary B) secondary C) tertiary D) quaternary
Which of the following is not known to be involved in the process of assisted folding of proteins? OA) Chaperonins OB) Disulfide interchange OC) Heat shock proteins OD) Peptide bond hydrolysis OE) Peptide bond isomerization
Please, help with the answer and explain it: When observing a bacterial cell, a scientist observed a chain forming attached to a ribosome. The chain absorbed a stain that was specific for amino acids, The chain that was forming was completely linear, representing which level of protein structure? protein? A) primary B) secondary C) tertiary D) quaternary
Which of the following features correctly describe aspects of protein structure? a) A protein possessing disulfide bonds will be more stable than a protein with the identical primary sequence lacking disulfide bonds. O b) B-sheets can only be formed from the anti-parallel arrangement of B-strands. c) Folding of a protein (tertiary structure) will typically result in a majority of the non-polar amino acids being distributed on the protein surface. d) both a and c
Protein kinases (PTKS) are enzymes that regulate the biological activity of proteins by phosphorylation of specific amino acids, inducing a conformational change from an inactive to an active form of the protein. a) True b) False

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