Serine and threonine can both be directly deaminated during amino acid metabolism. What else do these two amino acids have in common? Both are achiral hydrophobic amino acids. Both can be phosphorylated or glycosylated. Both destabilize beta sheets if they are incorporated into the secondary structure. Both readily form covalent disulfide bonds to stabilize a protein's tertiary structure.
Serine and threonine can both be directly deaminated during amino acid metabolism. What else do these two amino acids have in common? Both are achiral hydrophobic amino acids. Both can be phosphorylated or glycosylated. Both destabilize beta sheets if they are incorporated into the secondary structure. Both readily form covalent disulfide bonds to stabilize a protein's tertiary 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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![Serine and threonine can both be directly deaminated during amino acid
metabolism. What else do these two amino acids have in common?
Both are achiral hydrophobic amino acids.
Both can be phosphorylated or glycosylated.
Both destabilize beta sheets if they are incorporated into the secondary
structure.
Both readily form covalent disulfide bonds to stabilize a protein's tertiary
structure.](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F790403c6-3ff1-4e96-a049-b154822a3275%2F640efec7-f203-45b7-af27-17722434c220%2Fpay2fp4_processed.png&w=3840&q=75)
Transcribed Image Text:Serine and threonine can both be directly deaminated during amino acid
metabolism. What else do these two amino acids have in common?
Both are achiral hydrophobic amino acids.
Both can be phosphorylated or glycosylated.
Both destabilize beta sheets if they are incorporated into the secondary
structure.
Both readily form covalent disulfide bonds to stabilize a protein's tertiary
structure.
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