2026-04-17T06:40:25Zhttps://recercat.cat/oai/requestoai:recercat.cat:10256/123462024-06-18T13:35:19Zcom_2072_452955com_2072_2054col_2072_452958
RECERCAT
author
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
2024-06-18T13:35:19Z
2024-06-18T13:35:19Z
info:eu-repo/date/embargoEnd/2026-01-01info:eu-repo/date/embargoEnd/2026-01-012016
http://hdl.handle.net/10256/12346
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 moleculeThis work has been supported by Grants BFU2009-06935 and BIO2013-43517 from MINECO (Spain)
Tots els drets reservats info:eu-repo/semantics/embargoedAccess
Ribonuclease A
Ribonucleases
Enzims
Enzymes
Enginyeria de proteïnes
Protein engineering
Structural investigation of ribonuclease A conformational preferences using high pressure protein crystallography
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion