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
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Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...
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Protein folding results in a thermodynamically [favorable] conformation. In folded proteins, polar groups tend to be [on the exterior] of a protein. Likewise, hydrophobic groups tend to be [in the interior] of folded proteins to avoid [unfavorable] interactions with water. Disulfide bonds contribute to protein stability by [covalent bonding] the side chains of two [cysteine] residues that have been brought into close proximity by folding.
Transcribed Image Text:Protein folding results in a thermodynamically [favorable] conformation. In folded proteins, polar groups tend to be [on the exterior] of a protein. Likewise, hydrophobic groups tend to be [in the interior] of folded proteins to avoid [unfavorable] interactions with water. Disulfide bonds contribute to protein stability by [covalent bonding] the side chains of two [cysteine] residues that have been brought into close proximity by folding.
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