2026-04-13T02:56:11Zhttps://recercat.cat/oai/request

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

Structural investigation of ribonuclease A conformational preferences using high pressure protein crystallography Kurpiewska, Katarzyna Dziubek, Kamil Katrusiak, Andrzej Font i Sadurní, Josep Ribó i Panosa, Marc Vilanova i Brugués, Maria Lewiński, Krzysztof Ribonuclease A Ribonucleases Enzims Enzymes Enginyeria de proteïnes Protein engineering 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) 2024-06-18T13:35:19Z 2024-06-18T13:35:19Z 2024-06-18T13:35:19Z info:eu-repo/date/embargoEnd/2026-01-01 info:eu-repo/date/embargoEnd/2026-01-01 2016 info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://hdl.handle.net/10256/12346 info:eu-repo/semantics/altIdentifier/doi/10.1016/j.chemphys.2016.01.010 info:eu-repo/semantics/altIdentifier/issn/0301-0104 info:eu-repo/grantAgreement/MICINN//BFU2009-06935/ES/Bases Moleculares Del Plegamiento Y Citotoxicidad De Las Ribonucleasas Pancreaticas. Evaluacion De La Actividad Citotoxica Y Diseño De Estrategias Para Su Control Mediante Splicing Proteico./ info:eu-repo/grantAgreement/MINECO//BIO2013-43517-R/ES/RIBONUCLEASAS E INTEINAS COMO HERRAMIENTAS MOLECULARES PARA EL DESARROLLO DE FARMACOS ANTITUMORALES Y ESTUDIO DE PROTEINOPATIAS/ Tots els drets reservats info:eu-repo/semantics/embargoedAccess Elsevier © Chemical Physics, 2016, vol. 468, p. 53-62 Articles publicats (D-B)