Detailed insight can be obtained from proteins at and near the air-water interface using external reflection IR and circular dichroism techniques. Besides information on local protein concentrations and surface layer thickness, it is shown that beta-lactoglobulin displays a limited unfolding at the
Conformations of protected oligo(γ-methyl-L-glutamates) at the air–water interface
✍ Scribed by W. Hecq; R. Brasseur; J. Caspers; A. Loffet
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1976
- Tongue
- English
- Weight
- 240 KB
- Volume
- 15
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
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Conformations of Protected Oligo(y -methyl-L-glutamates) at the Air-Water Interface
Synopsis
In a previous paper dealing with the synthesis and the conformational behavior of a series of oligo(y-methyl-L-glutamates), it was shown that an organized conformation appeared a t approximately the heptapeptide level, the peptides being either dissolved in trifluoroethanol or spread a t the air-water interface.
The results were confirmed in the present work using the tritium-hydrogen exchange method and surface viscoelasticity measurements. The results suggest a conformational transition when the degree of polymerization of the spread peptides varies from six to eight.
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