Secondary Structure of Proteins Through Circular Dichroism Spectroscopy
✍ Scribed by Johnson, W C
- Book ID
- 111897105
- Publisher
- Annual Reviews
- Year
- 1988
- Tongue
- English
- Weight
- 731 KB
- Volume
- 17
- Category
- Article
- ISSN
- 0883-9182
No coin nor oath required. For personal study only.
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## 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
## Abstract Circular dichroism (CD) spectroscopy has been a valuable method for the analysis of protein secondary structures for many years. With the advent of synchrotron radiation circular dichroism (SRCD) and improvements in instrumentation for conventional CD, lower wavelength data are obtainab