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
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DOI：
10.1016/j.bbapap.2009.05.004
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发表时间：
2009-10-01
影响因子：
3.2
通讯作者：
Bellissent-Funel, M. -C.
中科院分区：
文献类型：
--
作者：
Appavou, M. -S.;Gibrat, G.;Bellissent-Funel, M. -C.
我们通过小角度中子散射研究了温度对溶液中BPTI结构的影响。我们已经研究了回旋半径的变化以及环境温度和368 K之间BPTI形状的修饰。结果表明，回旋半径从环境温度下的10.9 Angstrom在368 K处的13.3 Angstrom上增加。通过准层中子散射研究了溶液中BPTI的内部动力学。对中间散射功能的中子数据分析揭示了两个弛豫时间7和72分别与全局平移扩散运动和蛋白质的内部运动有关。已经检测到属于位于蛋白质表面的残基的侧链的质子的运动。将结果与最近发表的有关压力对溶液中BPTI结构和动力学的影响的结果进行了比较[Appavou MS等。 Biochimica et Biophysica Acta，1764，2006，pp 414-423]。 （c）2009 Elsevier B.V.保留所有权利。
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 angstrom at ambient temperature up to 13.3 angstrom 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 7, and 72 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]. (C) 2009 Elsevier B.V. All rights reserved.