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Article

Conformation and thermal denaturation of apocalmodulin: role of electrostatic mutations.

Biochemistry - 25 Feb 1997

Protasevich I, Ranjbar B, Lobachov V, Makarov A, Gilli R, Briand C, Lafitte D, Haiech J

Abstract excerpt

Scanning microcalorimetry and circular dichroism were used to study conformational state and heat denaturation of Ca2+-free synthetic calmodulin (SynCaM) and three charge reversal mutants. We produced evidence for the major role of the electrostatic potential in the stability and flexibility of SynCaM. The substitution of 118DEE120 by 118KKK120 (SynCaM12A) does not influence the flexibility of the protein; the...

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Identifiers

PMID: 9047299
DOI: 10.1021/bi962538g

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