Which of the following statement/s are incorrect?I. All amino acids are chiral.II. Essential amino acids are those that are used during translation.II. The a-carbons in a protein backbone are equally likely to have an R or S absolute configuration.O l and IIO l and IIIIl and IIO I, II, and IIIO None. All of the statements are correct.

Amino acids make up proteins. Amino acids are joined to each other by peptide bonds which are formed…

Answered: Which of the following statement/s are…

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

1. Sickle cell anemia results from a substitution of a valine for a glutamic acid. What do you expect the effect might be if the mutation were to have placed a leucine at that site? An aspartic acid? 2. Of the following amino acids, glycine, isoleucine, and lysine, which would you expect to be the most soluble in an acidic aqueous solution? Which the least? 3. How many structural isomers could be formed from a molecule with the formula C5H12? C4H8?
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Which of these mutations would you predict to be most detrimental? Explain your answer. (Refer to a chart of amino acid structures as necessary.) Asp to Glu Asn to Glu Cys to Lys Pro to Gly Val to Thr
5
6) Proline is not commonly found in the middle of a-helices because its ring structure prevents it from adopting the proper value and because it disrupts the hydrogen-bonding pattern of the helix. Looking at the structure of proline in the amino acid sequence below, suggest how this residue would disrupt the hydrogen-bonding pattern of an a-helix. 'N H R N N H *** R
10
Trypsin cleaves a polypeptide backbone at the C-terminal side of Arg or Lys residues, whereas chymotrypsin cleaves after aromatic residues. A polypeptide was treated with trypsin to generate a series of fragments of the following sequences: Gly-Gly-Ile-Arg Ser-Phe-Leu-Gly Trp-Ala-Ala-Pro-Lys Ala-Glu-Glu-Gly-Leu-Arg And the same polypeptide was treated with chymotrypsin to generate the following fragments: Leu-Gly Ala-Glu-Glu-Gly-Leu-Arg-Trp Ala-Ala-Pro-Lys-Gly-Gly-Ile-Arg-Ser-Phe Assemble the protein sequence.
A protein X is extensively methylated at lysine residues, converting it to protein Y. If the protein is to be separated by cation exchanger, what would be the order of elution? CAX, followed by Y OB. Y, followed by X OC. Both will be eluted at the same time O D. Both will bind with the matrix in the exchanger and will not elute out OE. A cation exchanger is not the ideal matrix for the separation
You want to translate a polycistronic bacterial MRNA in eukaryotic cells. You remove all stop codons except the last stop codon in the bacterial DNA before inserting it into the genome of a eukaryotic cell. Can you get a functional protein using this method? Yes or No. Briefly justify your answer.
What general structural feature is shared by proteins that specifically form homodimers (but not homotrimers, homoteramers etc)? Only one answer is correct. the surface consists of hydrophilic alpha-helix. the surface is highly modified by post-translational modification. the surface is permanently bound by chaperones. the surface is unstructured. the surface, or part of it, is self-complementary.
Explain how polypeptides are arranged to form the primary, secondary and tertiary structure of a protein how mutations can cause a change in the sequence of amino acids of a polypeptide? Compare the effects of addition/ deletion mutations and substitution mutations
1) what is the net charge of the amino acid leucine of it is on the C-terminus end and why? 2) if the amino acid was changed to lysine on the c-terminus end explain why and what the net charge would be?.

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