Normal Raman spectra were obtained for three crystalline forms of human insulin: 4Zn, 2Zn, and Zn-free or Na, from 1800-200 cm1. The extraction of a large number of component bands from the heavily overlapped Raman bands was accomplished by Fourier Self Deconvolution and bandfitting. Bands considered to be indicative of protein conformation, including Amide I, Amide III, tyrosine, 5-5, and C-S bands, and some which are relatively insensitive to protein structure, such as phenylalanine and histidine, are compared. The published x-ray structures of 4Zn and 2Zn insulins are used to help interpret the corresponding parameters of the extracted Raman bands, and to suggest structures in the as yet unpublished Na/human insulin crystals.

Date Published: 1 November 1990
PDF: 13 pages
Proc. SPIE 1336, Raman and Luminescence Spectroscopies in Technology II, (1 November 1990); doi: 10.1117/12.22913

Published in SPIE Proceedings Vol. 1336:
Raman and Luminescence Spectroscopies in Technology II
Fran Adar; James E. Griffiths, Editor(s)