3. Amino Acid Sequence and Protein Structure Our growingunderstanding of how proteins fold allows researchers to makepredictions about protein structure based on primary amino acidsequence data. Consider the following amino acid sequence.135678 910Ile - Ala - His - Thr - Tyr - Gly - Pro - Phe-Glu – Ala--11121314151720Ala - Mat - Cys- Lys - Trp - Glu-Ala-Gln-Pro - Asp-1618 192122232425262728Gly - 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. Explainyour reasoning.

Proteins are made up of amino acids that are linked together by peptide bonds. The simple linear…

Answered: (a) Where might bends or 3 turns occur?…

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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Similar questions

What does this statement mean: "Upon folding of a protein many main chain amides replace their hydrogen bonds to water for those with other amide bonds" Is this true for alpha helix in proline racemase? and is there a pattern?
A tetrameric protein dissociates into dimers when the detergent sodium dodecyl sulfate (SDS) is added to a solution of the protein. But the dimers are termed SDS-resistant because they do not further dissociate into monomers in the presence of the detergent. What intermolecular forces might be acting at the dimer-dimer interface? Are the intermolecular forces acting at the monomer-monomer interface different? Explain.
Consider the peptide in the image and answer the following questions.
Which of the following statements are False? (i) Parallel b-sheets characteristically distribute hydrophobic side chains on both sides of the sheet, and antiparallel B-sheets are usually arranged with all their hydrophobic residues on one side of the sheet. (ii) Planarity of the peptide bond means that no rotation occurs about the N-Ca bond while rotation is allowed about the C(O)-N and Ca-C(O) bonds. (iii) Silk fibers consist of fibroin proteins consisting of alternating A and G or S residues. (iv) If an aspartic acid residue were present in the interior of a globular protein, it would most likely be deprotonated and thus negatively charged.
Glutamine is an amino acid that has -CH₂-CH2-CO-NH₂ as its R group. The R group of the amino acid isoleucine is -CH2-CH-(CH3)2. If these amino acids were in a globular protein in aqueous solution, where would they most likely be? O Both glutamine and isoleucine would be in the interior and on the exterior of the globular protein. O Glutamine would be in the interior, and isoleucine would be on the exterior of the globular protein. O There isn't enough information O Both glutamine and isoleucine would be on the exterior of the globular protein. O Isoleucine would be in the interior, and glutamine would be on the exterior of the globular protein.
Draw the peptide formed between asparagine and histidine. H,N- -CH-C-OH H,N-CH-ċ-OH ČH2 ČH, N° NH2 -NH +
Consider protein folding that results when the following components interact: Where the solution is at a pH of 7, green (thick-dotted line) represents aspartic acid (R group contains a carboxylic acid with pKa = 4), orange (thick-solid line) represents lysine (R group contains an amine with pKa = 10), and blue (thin-solid line) represents hydrophilic groups. Rank the three complexes in order from lowest to highest dissociation constants Kd (low Kd values correspond to good binding constants and low energy, while high Kd values correspond to low binding constants and high energy) as determined by intermolecular charge-charge interactions. For those complexes with charge-charge interactions being equal, look at the possibility for the formation of hydrogen bonds via carboxylic acid dimers (only possible when the carboxylic acid is protonated) which are low energy structures.
If you were given the abbreviations for 4-6 amino acids, could you draw the polypeptide chain AND determine its isoelectric point? Do this for the amino acid Asp-Arg-Val-Tyr-Ile
can u help me

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