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 that accounts for homogeneous broadening and for the coupling with high- and low-frequency vibrational modes, while...
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