Description: Temperature dependence on structure and dynamics of Bovine Pancreatic Trypsin Inhibitor (BPTI) A neutron scattering study

This title appears in the Scientific Report : 2009

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...

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):	Animals Aprotinin: chemistry Cattle Models, Molecular Neutron Diffraction Protein Conformation Scattering, Small Angle Solutions Spectroscopy, Fourier Transform Infrared Temperature Thermodynamics Aprotinin J BPTI Small angle neutron scattering Quasielastic neutron scattering
	Publikationsportal JuSER

Please use the identifier: http://dx.doi.org/10.1016/j.bbapap.2009.05.004 in citations.

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].