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| Titel: |
The 31 Helix-Coil Transition for Polypeptides.: Circular Dichroism Studies |
| Auteur: |
Rippon, W. B. Lam, Rita |
| Verschenen in: |
International journal of polymeric materials |
| Paginering: | Jaargang 4 (1975) nr. 1-2 pagina's 25-32 |
| Jaar: |
1975-07-01 |
| Inhoud: |
Circular dichroism has become a popular method for following conformational transitions induced in optically active polymers. Recent refinement of experimental spectra obtained from model polypeptides by computer fitting to spectra obtained from solutions of proteins of known conformation has verified the applicability of the models chosen for the α helical and β conformations. However, the spectrum required for disordered regions was in conflict with much of the literature and agrees with our assignment based on studies of collagen and collagen models at elevated temperature. This spectrum consists of two troughs, one at ~225 nm and the other at ~200 nm. The latter had previously been associated with random polypeptides and we have shown the former to be sensitive to disorder in polymers approaching the 31 helical conformation. This paper presents the results from a study of three polypeptides which undergo a 31 helix → disorder transition. |
| Uitgever: |
Taylor & Francis |
| Bronbestand: |
Elektronische Wetenschappelijke Tijdschriften |
Details van artikel 6 van 6 gevonden artikelen
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