Abstract
Studies of the pressure dependence on protein structure and dynamics contribute not only to the basic knowledge of biological molecules but have also a considerable relevance in full technology, like in food sterilization and pharmacy. Conformational changes induced by pressure as well as the effects on the protein stability have been mostly studied by optical techniques (optical absorption, fluorescence, phosphorescence), and by NMR. Most optical techniques used so far give information related to the local nature of the used probe (fluorescent or phosphorescent tryptophan). Small angle neutron scattering and quasi-elastic neutron scattering provide essential complementary information to the optical data, giving quantitative data on change of conformation of soluble globular proteins such as bovine pancreatic trypsin inhibitor (BPTI) and on the mobility of protons belonging to the protein surface residues.
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Bellissent-Funel, MC., Appavou, MS., Gibrat, G. (2010). Effects of Pressure on Stability of Biomolecules in Solutions Studied by Neutron Scattering. In: Rzoska, S., Drozd-Rzoska, A., Mazur, V. (eds) Metastable Systems under Pressure. NATO Science for Peace and Security Series A: Chemistry and Biology. Springer, Dordrecht. https://doi.org/10.1007/978-90-481-3408-3_27
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DOI: https://doi.org/10.1007/978-90-481-3408-3_27
Publisher Name: Springer, Dordrecht
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