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.


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    Title :

    The structural organization of polypeptides at the air-water interface


    Contributors:

    Published in:

    Publication date :

    1987-01-01


    Size :

    3 pages




    Type of media :

    Article (Journal)


    Type of material :

    Electronic Resource


    Language :

    English




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