Article
Conformational changes in hemoglobin S (betaE6V) imposed by mutation of the beta Glu7-beta Lys132 salt bridge and detected by UV resonance Raman spectroscopy.
The Journal of biological chemistry - 28 Feb 2003
Juszczak Laura J, Fablet Christophe, Baudin-Creuza Veronique, Lesecq-Le Gall Sophie, Hirsch Rhoda Elison, Nagel Ronald L, Friedman Joel M, Pagnier Josee
Abstract excerpt
The impact upon molecular structure of an additional point mutation adjacent to the existing E6V mutation in sickle cell hemoglobin was probed spectroscopically. The UV resonance Raman results show that the conformational consequences of mutating the salt bridge pair, betaGlu(7)-betaLys(132), are dependent on which residue of the pair is modified. The betaK132A mutants exhibit the spectroscopic signatures of the...
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