The use of deuterium exchange for the study of the distortion of α-helices in proteins
✍ Scribed by Evgeni V. Brazhnikov; Yuri N. Chirgadze
- Book ID
- 118917961
- Publisher
- Elsevier Science
- Year
- 1978
- Tongue
- English
- Weight
- 648 KB
- Volume
- 122
- Category
- Article
- ISSN
- 0022-2836
No coin nor oath required. For personal study only.
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A ngeles, Los A nge les, California 90024 ## Synopsis Solvent accessible peptide bonds in proteins exhibit a 1-3" compression of the OCN bond angle and a corresponding expansion of the NCCa bond angle, relative to buried peptide bonds. These changes are consistent with an increase in hydrogen bon
## Abstract Experimental data are summarized on decay kinetics of uv‐induced paramagnetic centers in globular proteins. The PC decay rate in the absence of oxygen in α helical regions is shown to differ always by about two orders from that in nonhelical regions of the polypeptide chain. This effect