The structural organization of polypeptides at the air-water interface.
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 alpha-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 alpha-helical structure at suitable phase boundaries is likely to represent the earliest form of structural organization in polypeptides.
Taylor
J W
JW
Laboratory of Biological Chemistry and Biochemistry, Rockefeller University, New York 10021, USA.
D000388:Air; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry; D019418:Evolution, Chemical; D019143:Evolution, Molecular; D006728:Hormones / Q000737:chemistry; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry*; D014867:Water / Q000737:chemistry
D000596:Amino Acids; D006728:Hormones; D010455:Peptides; D014867:Water