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Conformation of Synthetic Polypeptide and Protein Monolayers at Interfaces

Abstract

SYNTHETIC polypeptide monolayers at the air–water interface are generally thought to be in extended-chain conformations1 though Bamford et al.2 have pointed out that the experimental data can often be interpreted as indicating the presence of the γ-helix3. Similarly, protein monolayers are usually considered to be denatured with the polypeptide chain fully extended4.

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References

  1. Cheesman, D. F., and Davies, J. T., Adv. Protein Chem., 9, 439 (Academic Press, New York, 1954).

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  2. Bamford, C. H., Elliott, A., and Hanby, W. E., Synthetic Polypeptides, 355 (Academic Press, New York, 1956).

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  3. Pauling, L., and Corey, R. B., Proc. U.S. Nat. Acad. Sci., 37, 235 (1951).

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  4. Adamson, A. W., Physical Chemistry of Surfaces (Interscience Pub., Inc., New York, 1960).

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  5. Elliott, A., and Hanby, W. E., Nature, 182, 654 (1958).

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  6. Doty, P., Rev. Mod. Phys., 31, 107 (1959).

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MALCOLM, B. Conformation of Synthetic Polypeptide and Protein Monolayers at Interfaces. Nature 195, 901–902 (1962). https://doi.org/10.1038/195901a0

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