This title appears in the Scientific Report :
2009
Please use the identifier:
http://dx.doi.org/10.1016/j.bbapap.2009.05.004 in citations.
Temperature dependence on structure and dynamics of Bovine Pancreatic Trypsin Inhibitor (BPTI) A neutron scattering study
Temperature dependence on structure and dynamics of Bovine Pancreatic Trypsin Inhibitor (BPTI) A neutron scattering study
We have studied the influence of temperature on the structure of BPTI in solution by small angle neutron scattering. We have investigated the variation of the radius of gyration and the modification of the shape of BPTI between ambient temperature and 368 K. Results have shown an increase of the rad...
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Personal Name(s): | Appavou, M.-S. |
---|---|
Gibrat, G. / Bellissent-Funel, M.C. | |
Contributing Institute: |
JCNS; JCNS Neutronenstreuung; IFF-5 Streumethoden; IFF-4 |
Published in: | Biochimica et biophysica acta, 1794 (2009) S. 1398 - 1406 |
Imprint: |
Amsterdam [u.a.]
Elsevier
2009
|
Physical Description: |
1398 - 1406 |
PubMed ID: |
19464393 |
DOI: |
10.1016/j.bbapap.2009.05.004 |
Document Type: |
Journal Article |
Research Program: |
Großgeräte für die Forschung mit Photonen, Neutronen und Ionen (PNI) Kondensierte Materie |
Series Title: |
Biochimica et Biophysica Acta
1794 |
Subject (ZB): | |
Publikationsportal JuSER |
We have studied the influence of temperature on the structure of BPTI in solution by small angle neutron scattering. We have investigated the variation of the radius of gyration and the modification of the shape of BPTI between ambient temperature and 368 K. Results have shown an increase of the radius of gyration from 10.9 A at ambient temperature up to 13.3 A at 368 K. Global and internal dynamics of BPTI in solution were studied by quasielastic neutron scattering. The analysis of neutron data in terms of intermediate scattering function reveals two relaxation times tau(1) and tau(2) related respectively to global translational diffusive motions and to internal motions of protein. Motions of protons belonging to lateral chains of residues located at the surface of the protein have been detected. The results are compared to the recently published results concerning the influence of pressure on structure and dynamics of BPTI in solution [Appavou MS et al. Biochimica et Biophysica Acta, 1764, 2006, pp 414-423]. |