客 **** Antiparallel B sheet Ala side chains Gly side chains **1 Figure 4-14a Lehninger Principles of Biochemistry, Seventh Edition 2017 W. H. Freeman and Company The structure of spider silk is shown above. Mutating the alanine residues to arginine is expected to disrupt the beta sheet structure. Please provide two reasons why mutating the alanine residues to arginine would be expected to disrupt the beta sheet structure.

客 ** Antiparallel B sheet Ala side chains Gly side chains 1 Figure 4-14a Lehninger Principles of Biochemistry, Seventh Edition 2017 W. H. Freeman and Company The structure of spider silk is shown above. Mutating the alanine residues to arginine is expected to disrupt the beta sheet structure. Please provide two reasons why mutating the alanine residues to arginine would be expected to disrupt the beta sheet structure.

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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I'm conducting an experiment concerned with the binding affinity of tretinoin (all trans retinoic acid) and beta lactoglobulin. This can be accomplished by monitorization of fluorescence quenching of a tryptophanyl residue that resides in a hydrophobic pocket known as a calyx inside the protein. Generally, fluorescence quenching is classified as static or dynamic. Would fluorescence quenching be a result of amide bond formation to tryptophan from tretinoin or through another mechanism (ie FRET: Forester resonance energy transfer)? Could it be both?
1CFD CALCIUM-FREE CALMODULIN How long is the protein’s primary sequence?Does this protein have any secondary, tertiary and/or quaternary structures present?Are there any molecular additions to this protein that are not amino ac
4. You're working on a structure of a protein and its folding. You think that the interaction between Asp123 and Arg29 is important in determining the structure of the protein. a) What type of amino acid is Asp (acidic, basic, hydrophobic, or polar)? b) What type of amino acid is Arg (acidic, basic, hydrophobic, or polar)? c) What is the strongest interaction that can form between Asp123 and Arg29? You create a mutant Arg29> Lys d) What type of amino acid is Lys (acidic, basic, hydrophobic, or polar)? e) Would you expect this substitution mutation to cause major folding problems? Why or why not? You create mutant Arg29> Glu you discover that this mutant is unable to fold properly, so the protein is nonfunctional. f What type of amino acid is Glu (acidic, basic, hydrophobic, or polar)? g) How does this amino acid substitution cause the protein to fold incorrectly? You find another mutant that also as the same Arg29> Glu mutation. However, this mutant protein įs able to fold normally.…
Hydrogen bonds are usually 2.7-3.3 angstrom long. According to this information, do you think there is a direct hydrogen bonding between H840 and the phosphodiester bond that links dG13 and dT14 (Chain C)? If not, what is the key role of H840 in Cas9?
Is there more than one subunit shown? Is your protein bound to anything else? Describe the secondary structures you see.
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
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A protein of unknown structure has been purified. Size-exclusion chromatography reveals that the native protein has a MW of 240,000. Chromatography in the presence of 6 M guanidine hydrochloride yields a single peak corresponding to a protein of MW 60,000. Chromatography in the presence of 6 M guanidine hydrochloride and 10 mM B-mercaptoethanol yields peaks for proteins of MW 34,000 and 26,000. Explain what can be determined about the structure of this protein from these data.