## Abstract To elucidate the structural characteristics of alcohol‐denatured proteins, we measured the vacuum‐ultraviolet circular dichroism (VUVCD) spectra of six proteins—myoglobin, human serum albumin, α‐lactalbumin, thioredoxin, β‐lactoglobulin, and α‐chymotrypsinogen A—down to 170 nm in triflu
Secondary-Structure Analysis of Denatured Proteins by Vacuum-Ultraviolet Circular Dichroism Spectroscopy
✍ Scribed by Matsuo, Koichi; Sakurada, Yoshie; Yonehara, Ryuta; Kataoka, Mikio; Gekko, Kunihiko
- Book ID
- 119921037
- Publisher
- Biophysical Society
- Year
- 2007
- Tongue
- English
- Weight
- 366 KB
- Volume
- 92
- Category
- Article
- ISSN
- 0006-3495
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We have expanded our reference set of proteins used in the estimation of protein secondary structure by CD spectroscopy from 29 to 37 proteins by including 3 additional globular proteins with known X-ray structure and 5 denatured proteins. We have also modified the self-consistent method for analyzi
The estimation of protein secondary structure from circular dichroism spectra is described by a multivariate linear model with noise (Gauss-Markoff model). With this formalism the adequacy of the linear model is investigated, paying special attention to the estimation of the error in the secondary s