ISSN:
0377-0486
Keywords:
Chemistry
;
Analytical Chemistry and Spectroscopy
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Chemistry and Pharmacology
,
Physics
Notes:
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.
Additional Material:
3 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/jrs.1250090506
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