Conformational stabilities of the rat alpha- and beta-parvalbumins.

doi:10.1016/s0014-5793(98)01666-4

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Article

Conformational stabilities of the rat alpha- and beta-parvalbumins.

FEBS letters - 15 Jan 1999

Henzl M T, Graham J S

Abstract excerpt

It is widely believed that beta-parvalbumin (PV) isoforms are intrinsically less stable than alpha-parvalbumins, due to greater electrostatic repulsion and an abbreviated C-terminal helix. However, when examined by differential scanning calorimetry, the apo-form of the rat beta-PV (i.e. oncomodul...

Topics

Animals
Calcium
Calorimetry, Differential Scanning
Escherichia coli
Hydrogen-Ion Concentration
Models, Molecular
Mutation
Osmolar Concentration
Parvalbumins
Protein Conformation
Protein Denaturation
Protein Isoforms
Rats
Recombinant Proteins
Static Electricity
Temperature
Thermodynamics

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