Which of the following is not known to be involved in the process of assisted folding ofproteins?OA) ChaperoninsOB) Disulfide interchangeOC) Heat shock proteinsOD) Peptide bond hydrolysisOE) Peptide bond isomerization

1 ) Disulfide interchange is not known to be involved in the process of assisted folding of proteins…

Answered: Which of the following is not known to…

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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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
Which of the following statements about electron microscopy are true? a) Most existing protein structures have been resolved using electron microscopy b) Electron microscopy is not used in structural biology as it can not give as high a resolution as X-ray crystallography and NMR c) The smaller a protein, the easier it is to solve its structure with electron microscopy d) By taking pictures of the same protein frozen in ice thousands of times and then adding them together, you get a high-resolution image of the protein e) The first protein structure with true atomic resolution was solved using electron microscopy last year
sugar and phosphate in a polynucleotide backbone are covalently linked by what? a) N-glucosidic bond b) phosphodiester bond c) peptide bond d) beta strand e) alpha helix
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
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.
An intermediate folding stage seen in protein denaturation or renaturation is called : a) domain b) motif c) subunit d) molten globule Proteins which do not renature spontaneously when denaturation conditions are removed may need the assistance of: a) a prosthetic group b) a higher salt concentration c) a lower temperature d) a chaperone protein The information needed for correct protein folding is encoded in: a) the surrounding molecules b) the protein’s amino acid sequence c) the pH of the aqueous medium d) the electrolyte composition of the aqueous solution
9) Which statement is inaccurate (wrong) about mRNA? A) it is double stranded and has thymine B) it can leave the nucleus C) It is single stranded and has uracil D) It is shorter than DNA 10) Which statemment accurately describes DDNA?
How is the secondary structure of a protein stabilized?a) Van der wall forcesb) Hydrogen bondingc) Covalent bondd) Hydrophobic bond
A sequence of amino acids in a certain protein is found to be -Ser-Gly-Pro-Gly-. The sequence is most probably part of a(n): A) parallel β sheet. B) α sheet. C) β turn. D) α helix. E) antiparallel β sheet.
Water-soluble proteins such as myoglobin tend to fold such that: A) hydrophobic amino acids R-groups are on the interior of the protein and hydrophilic groups are on the outside OB) all peptides form hydrogen bonds with water. C) hydrophilic amino acid R-groups are on the interior of the protein and hydrophobic groups are on the outside. O D) hydrophilic and hydrophobic amino acid R-groups form hydrogen bonds with each other.
1. ) In one (1) sentence point out a key structural similarity and difference in each of the following pair of terms: a) Proline and cysteine b) Secondary and Tertiary proteins c) Uracil and thymine d) AMP and dAMP e) codon and anticodon

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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