| License: Creative Commons Attribution 4.0 PDF - Published Version (1MB) |
- URN to cite this document:
- urn:nbn:de:bvb:355-epub-448282
- DOI to cite this document:
- 10.5283/epub.44828
This publication is part of the DEAL contract with Springer.
Abstract
For interpreting the pressure induced shifts of resonance lines of folded as well as unfolded proteins the availability of data from well-defined model systems is indispensable. Here, we report the pressure dependence of(1)H and(15)N chemical shifts of the side chain atoms in the protected tetrapeptides Ac-Gly-Gly-Xxx-Ala-NH2(Xxx is one of the 20 canonical amino acids) measured at 800 MHz proton ...

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