2026-04-17T12:31:27Zhttps://recercat.cat/oai/request

oai:recercat.cat:10256/123462024-06-18T13:35:19Zcom_2072_452955com_2072_2054col_2072_452958

00925njm 22002777a 4500 dc Kurpiewska, Katarzyna author Dziubek, Kamil author Katrusiak, Andrzej author Font i Sadurní, Josep author Ribó i Panosa, Marc author Vilanova i Brugués, Maria author Lewiński, Krzysztof author info:eu-repo/date/embargoEnd/2026-01-01 info:eu-repo/date/embargoEnd/2026-01-01 2016 Hydrostatic pressure in range 0.1-1.5 GPa is used to modify biological system behaviour mostly in biophysical studies of proteins in solution. Due to specific influence on the system equilibrium high pressure can act as a filter that enables to identify and investigate higher energy protein conformers. The idea of the presented experiments is to examine the behaviour of RNase A molecule under high pressure before and after introduction of destabilizing mutation. For the first time crystal structures of wild-type bovine pancreatic ribonuclease A and its markedly less stable variant modified at position Ile106 were determined at different pressures. X-ray diffraction experiments at high pressure showed that the secondary structure of RNase A is well preserved even beyond 0.67 GPa at room temperature. Detailed structural analysis of ribonuclease A conformation observed under high pressure revealed that pressure influences hydrogen bonds pattern, cavity size and packing of molecule This work has been supported by Grants BFU2009-06935 and BIO2013-43517 from MINECO (Spain) http://hdl.handle.net/10256/12346 Ribonuclease A Ribonucleases Enzims Enzymes Enginyeria de proteïnes Protein engineering Structural investigation of ribonuclease A conformational preferences using high pressure protein crystallography