betaME on protein structure. The proteins don't contain any cysteine residues in its primary structure A.) It breaks disulfide bonds B.) It binds covalently to sidechains that contain OH groups, leading to protein denaturation C.) It denatures proteins by changing the solvent properties so that the hydrophobic ffect is are:
betaME on protein structure. The proteins don't contain any cysteine residues in its primary structure A.) It breaks disulfide bonds B.) It binds covalently to sidechains that contain OH groups, leading to protein denaturation C.) It denatures proteins by changing the solvent properties so that the hydrophobic ffect is are:
Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:Elaine N. Marieb, Katja N. Hoehn
Chapter1: The Human Body: An Orientation
Section: Chapter Questions
Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...
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Transcribed Image Text:5.) Which one best describes the effect of
betaME on protein structure. The proteins
don't contain any cysteine residues in its
primary structure
A.) It breaks disulfide bonds
B.) It binds covalently to sidechains that
contain OH groups, leading to protein
denaturation
C.) It denatures proteins by changing the
solvent properties so that the hydrophobic
effect is greatly reduced
D.)It breaks peptide bonds
E.) It denatures proteins by protonating
groups
Transcribed Image Text:which in is the best method for separating
proteins A and B that have the properties
below:
Protein A: a tetramer of identical 80kDa
subunits with a pl of 6.4
Protein B: a monomeric protein with a MW of
80kDa and a pl of 9.2
A.) Anion exchange chromatography at pH 11
B.) Gel exclusion chromatography
C.) Cation exchange chromatography at pH 4
D. Cation exchange chromatography at pH 11
E.) SDS-PAGE
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