Dynamic properties of some beta-chain mutant hemoglobins.

doi:10.1002/prot.340220103

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Article

Dynamic properties of some beta-chain mutant hemoglobins.

Proteins - 1 May 1995

Militello V, Cupane A, Leone M, Brinigar W S, Lu A L, Fronticelli C

Abstract excerpt

The thermal behavior of the Soret band relative to the carbonmonoxy derivatives of some beta-chain mutant hemoglobins is studied in the temperature range 300-10 K and compared to that of wild-type carbonmonoxy hemoglobin. The band profile at various temperatures is modeled as a Voigt function tha...

Topics

Base Sequence
Carboxyhemoglobin
Cold Temperature
Heme
Hemoglobin A
Models, Chemical
Molecular Sequence Data
Mutagenesis, Site-Directed
Mutation
Recombinant Proteins
Spectrophotometry

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