. A protein has been sequenced after cleavage of disulfide bonds. The protein is known to contain 3 Cys residues, located as shown below. Only one of the Cys has a free - SH group and the other two are involved in an -s-s- bond. A Phe Cys « N-terminus Cys- - Met Cys- C-terminus The only methionine and the only aromatic amino acid (Phe) in this protein are in the positions indicated. Cleavage of the intact protein (i.e., with disulfide bonds intact) by either cyanogen bromide or chymotrypsin does not break the protein into two peptides. Where is the -s-s- bond (i.e., AB, BC, or AC)?

. A protein has been sequenced after cleavage of disulfide bonds. The protein is known to contain 3 Cys residues, located as shown below. Only one of the Cys has a free - SH group and the other two are involved in an -s-s- bond. A Phe Cys « N-terminus Cys- - Met Cys- C-terminus The only methionine and the only aromatic amino acid (Phe) in this protein are in the positions indicated. Cleavage of the intact protein (i.e., with disulfide bonds intact) by either cyanogen bromide or chymotrypsin does not break the protein into two peptides. Where is the -s-s- bond (i.e., AB, BC, or AC)?

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter31: Completing The Protein Life Cycle: Folding, Processing, And Degradation

Section: Chapter Questions

Problem 3P: Understanding the Relevance of Chaperones in Protein Folding Protein molecules, like all molecules,...

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A protein has been sequenced after cleavage of disulfide bonds. The protein is known to contain 3 Cys residues, located as shown here. Only one of the Cys has a free —SH group, and the other two are involved in an —S—S— bond. The only methionine and the only aromatic amino acid (Phe) in this protein are in the positions indicated. Cleavage of the intact protein (i.e., withdisulfide bonds intact) by either cyanogen bromide or chymotrypsin does not break the protein into two peptides. Where is the —S—S— bond (i.e., AB, BC, or AC)?
Which statements are true? Explain why or why not.1 Each strand in a β sheet is a helix with two aminoacids per turn.2 Intrinsically disordered regions of proteins can beidentified using bioinformatic methods to search genes forencoded amino acid sequences that possess high hydro-phobicity and low net charge.3 Loops of polypeptide that protrude from the sur-face of a protein often form the binding sites for other mol-ecules.4 An enzyme reaches a maximum rate at high sub-strate concentration because it has a fixed number ofactive sites where substrate binds.5 Higher concentrations of enzyme give rise to ahigher turnover number.6 Enzymes that undergo cooperative allosteric tran-sitions invariably consist of symmetric assemblies of mul-tiple subunits.7 Continual addition and removal of phosphatesby protein kinases and protein phosphatases is wastefulof energy—since their combined action consumes ATP—but it is a necessary consequence of effective regulation byphosphorylation.
The three-dimensional conformation of a protein may be strongly influenced by amino acid residues that are very far apart in sequence. This relationship is in contrast to secondary structure, where the amino acid residues are: a. always side by side. b. generally near each other in sequence. c. invariably restricted to about 7 of the 20 standard amino acids. d. often on different polypeptide strands. e. usually near the polypeptide chain's amino terminus or carboxyl terminus.
2. A ligand binds more tightly to the folded state (N) of a protein than to the unfolded state (U). Show that the ligand stabilizes the protein and calculate by how much (ΔΔGfold = ?). Please help me find out deltadelta G fold.
Which of the following statements best describe(s) the mechanism by which correct protein folding takes place once the misfolded protein binds the open ring of groEL? Select all that apply. The groEL ring closes to isolate the protein and provide enough time for the protein to properly fold on its own. b and d The groEL ring closes to provide a hydrophilic space to isolate the protein and inhibit its aggregation with others until properly folded. The groEL ring closes to isolate the protein and provide steric hindrance that mechanically refolds the protein. The groEL ring closes to isolate the protein and decode the information necessary to achieve the correct three-dimensional structure. None of the above I picked "The groEL ring closes to provide a hydrophilic space..." but it was incorrect..
Gene editing is also used to explore the structure and function ofproteins. For example, changes can be made to the coding sequenceof a gene to determine how alterations in the amino acid sequenceaffect the function of a protein. Let’s suppose that you areinterested in the functional importance of a particular glutamicacid (an amino acid) within a protein you are studying. By geneediting, you make mutant proteins in which the glutamic acidcodon has been changed to other codons. You then test the encodedmutant proteins for functionality. The results are as follows: FunctionalityNormal protein 100%Mutant proteins containingTyrosine 5%Phenylalanine 3%Aspartic acid 94%Glycine 4%From these results, what would you conclude about the…
What following statement is TRUE concerning motifs and domains? a) Both motifs and domains are independently stable. b) Domains undergo dynamic individual changes that affect the entire protein c) B-a-ß loops, B barrels, and helix-turn-helix structure are types of domains d) Motifs and domains are part of secondary structural elements e) Ab initio computations predict motif folds accurately a majority of the time My guess is B.
Show below is a polypeptide comprised of 3 α-helices and 5 β-sheets joined by randomcoil. Characterizetheforces that stabilize the tertiarystructure and draw the interacting side chains ofd) Cys Cys
1. What is the isoelectric point (pI) of lysine which has pKa values of 2.1 for the α carboxyl group, 9.7 for the α amino group and 10.5 for the side chain amino group? 2. Which of the following is most likely to be found on the exterior of a protein? A) Pro B) Trp C) Ser D) Glu 3. The type of reaction that forms a peptide bond is A) Elimination B) Hydrolysis C) Nucleophilic substitution D) Condensation
Does your protein 3GRS have a quaternary structure??? talk about the tertiary structure of 3GRS. https://www.rcsb.org/
Which of the following statements are correct about the role of chaperones in protein folding (select all that appy)? A. Chaperones accelerate the rate of protein folding B. Presence of chaperones contradicts dogma that structure of protein is only determined by amino acid sequence C. Chapreone promotion of native folding is an ATP-dependent process D. Chaperones work by stabilizing hydrophobic patches on proteins E. A cell line with the GroEL and GroES deleted would accumulate more unfolded protein
Suppose you have a solution of a protein, which contains a specific Tyr residue that has an actual (measured) pKa of 8.8. The protein binds a ligand by several noncovalent interactions, one of which is a hydrogen bond in which the Tyr phenolic hydroxyl group must serve as a hydrogen bond donor. Calculate the percentage of the protein molecules in which that tyrosyl residue's phenolic hydroxyl group could serve as a hydrogen bond donor at pH 8.5