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Article

Stability of monomeric Cro variants: Isoenergetic transformation of a type I' to a type II' beta-hairpin by single amino acid replacements.

Protein science : a publication of the Protein Society - 1 May 2003

Mollah A K M M, Stennis Rhonda L, Mossing Michael C

Abstract excerpt

The thermodynamic stabilities of three monomeric variants of the bacteriophage lambda Cro repressor that differ only in the sequence of two amino acids at the apex of an engineered beta-hairpin have been determined. The sequences of the turns are EVK-XX-EVK, where the two central residues are DG, GG, and GT, respectively. Standard-state unfolding free energies, determined from circular dichroism measurements as a...

Topics

Amino Acid Sequence
Amino Acid Substitution
DNA-Binding Proteins
Genetic Variation
Protein Denaturation
Protein Structure, Secondary
Repressor Proteins
Thermodynamics
Viral Proteins
Viral Regulatory and Accessory Proteins

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Identifiers

PMID: 12717034
DOI: 10.1110/ps.0239003
PMCID: PMC2323882

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