Protein folding results in a thermodynamically conformation. In folded proteins, polar groups tend to be of a protein. Likewise, hydrophobic groups tend to be of folded proteins to avoid interactions with water. Disulfide bonds contribute to protein stability by the side chains of two residues that have been brought into close proximity by folding.
Protein folding results in a thermodynamically conformation. In folded proteins, polar groups tend to be of a protein. Likewise, hydrophobic groups tend to be of folded proteins to avoid interactions with water. Disulfide bonds contribute to protein stability by the side chains of two residues that have been brought into close proximity by folding.
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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i had gotten them all right except for one, just need to compare what you have versus my answers
Transcribed Image Text:glycine
Protein folding results in a thermodynamically
conformation. In folded proteins, polar
ionic bonding
groups tend to be
of a protein. Likewise, hydrophobic groups tend to be
lysine
of folded proteins to avoid
interactions with water. Disulfide bonds
contribute to protein stability by
the side chains of two
residues that
covalent bonding
have been brought into close proximity by folding.
unfavorable
hydrogen bonding
in the interior
on the exterior
cysteine
favorable
methionine
Supmit
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