Document Detail


Fourier transform infrared spectroscopic study of molecular interactions in hemoglobin.
MedLine Citation:
PMID:  20203908     Owner:  NLM     Status:  In-Data-Review    
Abstract/OtherAbstract:
Infrared absorption spectra of the alpha-104 (G11) cysteine SH group have been observed for aqueous solutions of hemoglobin derivatives from humans, pigs, and horses. The center frequencies ((nu)SH) show ligand sensitive patterns that are similar for the three species, with (nu)SH (HbCO) <(nu)SH (HbO(2) ~ HbCN) < (nu)SH (Hb(+)) <<(nu)SH (deoxyHb) for human and pig hemoglobins. The alpha-104 SH group is most strongly H-bonded (smallest (nu)SH), has the greatest range of (nu)SH (Hb ? HbCO) in human hemoglobin, and is least strongly H-bonded and has the smallest range of (nu)SH (Hb ? HbCO) in horse hemoglobin. The beta-112 cysteine SH in human hemoglobin is more weakly H-bonded than is the alpha-104 SH. These studies illustrate how FTIR can be used to measure differences in protein structure that are related to biological control mechanisms.
Authors:
J O Alben; G H Bare
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Applied optics     Volume:  17     ISSN:  0003-6935     ISO Abbreviation:  Appl Opt     Publication Date:  1978 Sep 
Date Detail:
Created Date:  2010-03-05     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0247660     Medline TA:  Appl Opt     Country:  United States    
Other Details:
Languages:  eng     Pagination:  2985-90     Citation Subset:  -    
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