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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Pressure dependence of backbone chemical shifts in the model peptides Ac-Gly-Gly-Xxx-Ala-NH2

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Erlach, Markus Beck [1, 2] ; Koehler, Joerg [1, 2] ; Crusca, Jr., Edson [3] ; Kremer, Werner [1, 2] ; Munte, Claudia E. [3] ; Kalbitzer, Hans Robert [1, 2]
Total Authors: 6
[1] Univ Regensburg, Inst Biophys & Phys Biochem, D-93040 Regensburg - Germany
[2] Univ Regensburg, Ctr Magnet Resonance Chem & Biomed, D-93040 Regensburg - Germany
[3] Univ Sao Paulo, Phys Inst Sao Carlos, BR-13566590 Sao Carlos, SP - Brazil
Total Affiliations: 3
Document type: Journal article
Source: Journal of Biomolecular NMR; v. 65, n. 2, p. 65-77, JUN 2016.
Web of Science Citations: 7

For a better understanding of nuclear magnetic resonance (NMR) detected pressure responses of folded as well as unstructured proteins the availability of data from well-defined model systems are indispensable. In this work we report the pressure dependence of chemical shifts of the backbone atoms H-1(alpha), C-13(alpha) and C-13' in the protected tetrapeptides Ac-Gly-Gly-Xxx-Ala-NH2 (Xxx one of the 20 canonical amino acids). Contrary to expectation the chemical shifts of these nuclei have a nonlinear dependence on pressure in the range from 0.1 to 200 MPa. The polynomial pressure coefficients B (1) and B (2) are dependent on the type of amino acid studied. The coefficients of a given nucleus show significant linear correlations suggesting that the NMR observable pressure effects in the different amino acids have at least partly the same physical cause. In line with this observation the magnitude of the second order coefficients of nuclei being direct neighbors in the chemical structure are also weakly correlated. (AU)

FAPESP's process: 10/01362-5 - Interaction of proteins with lipidic microdomains and biological membrane models
Grantee:Claudia Elisabeth Munte
Support type: Regular Research Grants
FAPESP's process: 10/12953-4 - Structural determination of the C-terminal domains of septins SEPT2 and SEPT4 and protein interaction with alpha-synuclein by NMR
Grantee:Edson Crusca Junior
Support type: Scholarships in Brazil - Post-Doctorate