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Comparative conformational studies of polypeptides containing a high percentage of proline
In the search for models of a proline-rich protein isolated from human parotid saliva the authors were led to synthesize and study H-(Gly-(Pro) sub(x)) sub(n)-OH (x = 3,4). Preliminary results concerning these polypeptides have already been reported and suggest that in aqueous solution these peptide...
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Published in: | Macromolecules 1981-05, Vol.14 (3), p.617-620 |
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Main Authors: | , |
Format: | Article |
Language: | English |
Subjects: | |
Online Access: | Get full text |
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Summary: | In the search for models of a proline-rich protein isolated from human parotid saliva the authors were led to synthesize and study H-(Gly-(Pro) sub(x)) sub(n)-OH (x = 3,4). Preliminary results concerning these polypeptides have already been reported and suggest that in aqueous solution these peptides adopt a polyproline II (PPII) conformation in addition to some other structures (probably unordered). In this paper the authors present a new synthesis of these products and a more complete conformational study comparing the relative stabilities of the PPII helix adopted by these polymers. |
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ISSN: | 0024-9297 1520-5835 |
DOI: | 10.1021/ma50004a032 |