Abstract The surface pressure-area isotherms generated by compressing monolayers formed by five polypeptide hormones at the air-water interface were studied. The results indicate that amphiphilic α-helical structures occupy the interfacial area, in agreement with predictions based only on the arrangements of the hydrophilic and hydrophobic amino-acid residues in the linear sequences of these polypeptides. The variety of such arrangements which result in the formation of stable helical structure, and their low degree of self-association, suggest that the induction of amphiphilic α-helical structure at suitable phase boundaries is likely to represent the earliest form of structural organization in polypeptides.
The structural organization of polypeptides at the air-water interface
Advances in Space Research ; 6 , 11 ; 19-21
1987-01-01
3 pages
Article (Journal)
Electronic Resource
English
British Library Online Contents | 2013
|NMR studies of prebiotic polypeptides
Online Contents | 1975
|Organization for a parallel optical memory interface
British Library Conference Proceedings | 1995
|Response to comments on thermal polypeptides
NTRS | 1976
|Synthesis of Sequential Polypeptides Containing O-Phospho-L-Serine
British Library Online Contents | 2003
|