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- URN to cite this document:
- urn:nbn:de:bvb:355-epub-295117
- DOI to cite this document:
- 10.5283/epub.29511
Abstract
High pressure NMR spectroscopy has developed into an important tool for studying conformational equilibria of proteins in solution. We have studied the amide proton and nitrogen chemical shifts of the 20 canonical amino acids X in the random-coil model peptide Ac-Gly-Gly-X-Ala-NH2, in a pressure range from 0.1 to 200 MPa, at a proton resonance frequency of 800 MHz. The obtained data allowed the ...
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