Imagine the main chain of a protein bends back on itself, so that two amino acid residues R₁ and R₂ come close to each other. Here's what R₁ looks like:-CH-CH₂CH₂CH₂CH₂1NH3Could R₁ form a salt bridge with R₂ at physiological pH, if R₂ were the right kind of residue?O yesO noIf you said R₁ could form a sal bridge with R₂, what would R₂ have to be?0If there's only one possibility, write its 3-letter code. If there is more than one possibility, write the3-letter code of any of them.X?BEET号图Ar

Salt bridge is a bond between amino acids which carry opposite charges. The opposite charges exert…

Answered: Imagine the main chain of a protein…

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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Imagine the main chain of a protein bends back on itself, so that two amino acid residues R, and R, come close to each other. Here's what R looks like: -CH- CH HO CH O yes Could R, form a salt bridge with R, at physiological pH, if R₂ were the right kind of residue? O no If you said R, could form a salt bridge with R₂, what would R, have to be? If there's only one possibility, write its 3-letter code. If there is more than one possibility, write the 3-letter code of any of them. Explanation Check Z X E all option H cmd H N J 0 O P cmd option
Suppose that there is a protein consisting of two polypeptide chains with the given sequences in the picture. What will be the expected result if a biochemist does an end-group analysis to identify the N and C terminal residues of the protein? Explain why.
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Imagine the main chain of a protein bends back on itself, so that two amino acid residues R, and R, come close to each other. In the table below are four possibilities for what R, and R, might be. In each case, decide whether a specific interaction could form between the residues. If a specific interaction could form, give the name of the interaction. R₁ R₂ threonine cysteine glutamine arginine cysteine tyrosine phenylalanine glutamate specific interaction? Oyes no yes O no O yes O no Oyes O no name of specific interaction 0 0 0 0 X
Which of the following amino acids are more likely to be on the interior of the protein? And which are more likely to be exposed to the surface? L I D E W A V K H M Q Y
which two amino acid have two chiral center？ I know Isoleucine contain two chiral center，how about another AA？
Amino acids project from each polypeptide backbone in a β-sheet in an alternating fashion (oneabove the plane and the next below the plane – see Fig 3.8B). Consider the following proteinsequence: Leu-Lys-Val-Asp-Ile-Ser-Leu-Arg-Leu-Lys-Ile-Arg-Phe-Glu.a. Is there a pattern to these amino acids? If so, what is it? b. What does this sequence of amino acids mean for the hydrophobicity/hydrophilicity of theresulting β-sheet? c. Can you make a prediction about how the β-sheet will be arranged in higher levels of protein structure? If so, what prediction would you make?
Draw the oligopeptides' structure and provide the corresponding name for each oligopeptide 1. Dipeptide Ala-His 2. Tripeptide Glu-Pro-Cys Note: First residue is the N-terminal amino acid
+H₂N-CH-COO™ T CH₂ I CH₂ 1 CH₂ I +H₂N-CH₂ A. O amino acid C amino acid D O amino acid E amino acid B +H₂N-CH-COO™ I CH₂ I CH₂ 1 O amino acid A C=0 B. If the pH decreases enough, this amino acid will become protonated and could contribute to the denaturation of the protein. +H₂N-CH-COO™ 1 CH₂ I OH C. +H₂N-CH-COO™ CH H₂C CH3 D.
In case of the same amino acid as in the picture, in which ionization state would this amino acid be at (i) a pH that will correspond with the pI-value and (ii) a pH below the pI-value?
Which amino acids would you expect to find marked on the alpha helix? Alanine Isoleucine Leucine Methionine Phenylalanine Tryptophan Valine 000000 |||| |||||| ||||||||| 000000 Nonpolar side chains; hydrophobic Side chain (R group) H₂N H₂N C 0 H₂N HO Glycine (Gly or G) CH₂ H₂N CH₂ CH₂ OH CH₂ CH₂ Methionine (Met or M) Polar side chains; hydrophilic HO Alanine (Ala or A) CH₂ H.Nº C C-O HO Phenylalanine (Phe or F) ỖI 0-0 SH он сн CH₂ CH OH₂NCCO H₂N*CCO Acidic (negatively charged) 0 0 Serine Threonine Cysteine (Ser or S) (Thr or T) (Cys or C) Electrically charged side chains; hydrophilic CH₂ CH₂ CH₂ CH₂ CH H₂NCCO H₂NCCO H₂NCC o HO Aspartic acid Glutamic acid (Asp or D) (Glu or E) HO Valine (Val or V) 000000000 ||||| ||||| ||||||| 00000000 NH₂ OH H₂N HẲN Ô CÓ HO Tryptophan (Trp or W) CH₂ H₂N² сCO 0 CH₂ CH₂ H₂NCCO HO Lysine (Lys or K) 0 Leucine (Leu or L) NH CH₂ CH₂ CH CH₂ NH₂ H₂N® CH₂ Tyrosine (Tyr or Y) Asparagine (Asn or N) Basic (positively charged) NH₂ CNH, NH CH₂ CH₂ CH₂ H₂NCCO HO…
The different types of interactions that stabilize the protein tertiary structure are illustrated in the diagram below. Which type of interaction moves some part of the polypeptide chain toward the inside of the folded protein? OH Hydrophilic OH CH₂ interaction with water Hydrogen bond -NH₂3-0- C Salt bridge -CH₂-OH C=0 H-N H 0-CH,- I H Hydrogen bond Salt bridge O Disulfide bond 222 -SIS Hydrophobic interaction 200 O Hydrogen bond O Hydrophilic interaction Disulfide bonds B-Pleated sheet O Hydrophobic interaction CH₂ CH₂ a Helix CH3 CH3 Hydrogen bonds

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