DQuestion 9I am an alanine residue present in a peptide with defined secondary structure. I haveand dihedral angles of 45° and -45°, respectively. What structure best defines myenvironment?O B-sheetO B-turnRight handed a-helixO Left handed a-helixO These angles do not correspond to a well-defined secondary structure

Introduction Proteins are the most abundant macromolecule of our body. Amino acids are the building…

Answered: Question 9 I am an alanine residue…

Biology 2e

2nd Edition

ISBN:9781947172517

Author:Matthew Douglas, Jung Choi, Mary Ann Clark

Publisher:Matthew Douglas, Jung Choi, Mary Ann Clark

Chapter3: Biological Macromolecules

Section: Chapter Questions

Problem 23CTQ: Amino acids have the generic structure seen below, where R represents different carbon-based side...

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Similar questions

Amino acids have the generic structure seen below, where R represents different carbon-based side chains. Describe how the structure of amino acids allows them to be linked into long peptide chains to form proteins.
The first and major effect in denaturation of proteins is that: a. peptide bonds break. b. helices unwind. c. sheet structures unfold. d. tertiary structure is changed. e. quaternary structures disassemble.
Protein: HemoglobinCircle and underline each codon, amino acid sequence, make a mutation of the 3rd codon in the nucleotide sequence and circle the affected areas , show the amino acid area with the mutation.Lasltyly describe the impact on the protein."MVHLTPEEKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLSTPDAVMGNPKVKAHGKKVLGAFSDGLAHLDNLKGTFATLSELHCDKLHVDPENFR"
Which of the following peptides is more likely to take up an α-helical structure, and why?(a) LKAENDEAARAMSEA(b) CRAGGFPWDQPGTSN
My PDB code: 3GRS residue point: HIS467 mutation: LEU Describe why this position in your protein is important and outline the effects the mutation will have on the 3D structure and the function of your protein. (up to 50 words)
1. Which peptide would be more soluble at pH 7.0, (Val)₂₀ or (Asp)₂₀ ? at pH 3.0, (Gly-Glu-Val)
A peptide with 12 amino acids has the composition (not sequence) Asp 2Cys 2Glu 2Leu 2Ser 2Tyr Val. It also has Ser as the N-terminal residue and Cys as C-terminal. Partial acid hydrolysis gave these peptide sequences: (a) SerLeuTyr (b) TyrCys (c) LeuTyrGlu (d) GluLeuGlu (e) SerValCys (f) CysSerVal (g) GluAspTyr . What is the peptide sequence?
don't copy 6. A protein-ligand binding reaction is run. At equilibrium, half the protein is ligand bound, the unboundligand concentration is 0.657 nM. Calculate the koff value for this reaction. Assume the kon value is typical ofprotein-ligand interactions.
Draw out this peptide using condensed or line-bond structures: His-Thy-Phe-Cys-Glu examine your drawing of peptide for each amino acid, indicate what type(s) of interactions it can contribute to protein tertiary structure
Please ASAP. Thank you. How does the mutation change/affect the structure of the Hb heterotetramer (ie how is quaternary protein structure affected)?
A sample of an unknown peptide was dividedinto two aliquots. One aliquot was treated with trypsin; the otherwas treated with cyanogen bromide. Given the following sequences(N-terminal to C-terminal) of the resulting fragments, deduce thesequence of the original peptide.
24. The sidechain of the amino acid serine is -CH2-OH. Serine is classified as this type of amino acid (side chain): a) hydrophobic and nonpolar b) hydrophilic and polar c) acidic d) basic

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