By Denise R. Ferrier
Lippincott’s Illustrated experiences: Biochemistry is the normal first-and top source for the necessities of biochemistry. scholars depend on this article to assist them speedy review, assimilate, and integrate quite a lot of serious and complicated info. For greater than twenty years, school and scholars have praised LIR Biochemistry’s matchless illustrations that make options come to life.NEW! • vast revisions and up-to-date content
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Additional info for Biochemistry (Lippincott's Illustrated Reviews Series)
This prevents free rotation around the bond between the carbonyl carbon and the nitrogen of the peptide bond. However, the bonds between the α-carbons and the α-amino or α-carboxyl groups can be freely rotated (although they are limited by the size and character of the R groups). This allows the polypeptide chain to assume a variety of possible configurations. 2B), in large part because of steric interference of the R groups when in the cis position. 3. Polarity of the peptide bond: Like all amide linkages, the – C =O and – NH groups of the peptide bond are uncharged and neither accept nor release protons over the pH range of 2–12.
2 A. Formation of a peptide bond, showing the structure of the dipeptide valylalanine. B. Characteristics of the peptide bond. B. Determination of the amino acid composition of a polypeptide The first step in determining the primary structure of a polypeptide is to identify and quantitate its constituent amino acids. A purified sample of the polypeptide to be analyzed is first hydrolyzed by strong acid at 110°C for 24 hours. This treatment cleaves the peptide bonds and releases the individual amino acids, which can be separated by cation-exchange chromatography.
Quaternary structure requires more than one polypeptide, and, when present, it is stabilized primarily by noncovalent bonds. The peptide bond is almost always trans. The two cysteine residues participating in disulfide bond formation may be a great distance apart in the amino acid sequence of a polypeptide (or on two separate polypeptides) but are brought into close proximity by the three-dimensional folding of the polypeptide. Denaturation may be reversible or irreversible. 2 A particular point mutation results in disruption of the α-helical structure in a segment of the mutant protein.
Biochemistry (Lippincott's Illustrated Reviews Series) by Denise R. Ferrier