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Laser excited Raman spectroscopy of biomolecules. 13—conformational study of α‐chymotrypsin and trypsin
Author(s) -
Chen Michael C.,
Lord R. C.
Publication year - 1980
Publication title -
journal of raman spectroscopy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.748
H-Index - 110
eISSN - 1097-4555
pISSN - 0377-0486
DOI - 10.1002/jrs.1250090506
Subject(s) - chymotrypsin , chemistry , trypsin , raman spectroscopy , biomolecule , aqueous solution , molecule , crystallography , excited state , spectroscopy , amide , hydrogen bond , analytical chemistry (journal) , enzyme , chromatography , organic chemistry , biochemistry , physics , quantum mechanics , nuclear physics , optics
The Raman spectra of bovine pancreatic α‐chymotrypsin and trypsin were determined from 7% aqueous solutions and lyophilized solids containing residual sulfate ion. A large amount of β‐pleated‐sheet structure is present in both molecules, as shown by the contour of the amide III region, but trypsin contains substantially more α‐helical conformation than does chymotrypsin. There is evidence of some change in structure of both molecules in solution as compared with the solids. The tyrosines are all or nearly all weakly hydrogen bonded in both enzymes, and the binding of sulfate ion is also weak in the lyophilized solids.