000131536 001__ 131536
000131536 005__ 20240212142201.0
000131536 0247_ $$2doi$$a10.1016/j.abb.2020.108323
000131536 0248_ $$2sideral$$a117167
000131536 037__ $$aART-2020-117167
000131536 041__ $$aeng
000131536 100__ $$0(orcid)0000-0002-1827-1250$$aGarcía-Rubio, Inés$$uUniversidad de Zaragoza
000131536 245__ $$aEPR of site-directed spin-labeled proteins: A powerful tool to study structural flexibility
000131536 260__ $$c2020
000131536 5060_ $$aAccess copy available to the general public$$fUnrestricted
000131536 5203_ $$aElectron Paramagnetic Resonance is a spectroscopic technique which, in combination with site-directed spin-labeling, provides structural and dynamic information about proteins in conditions similar to those of their physiological environment. The information is sequence-resolved, as it is based on probing the local dynamics of a paramagnetic label incorporated as a side chain of a selected amino acid. EPR does not impose a limit on the size of the protein or protein complex, as long as it is amenable to site-directed mutagenesis, and is able to obtain reliable distance distributions between two or more labels (identical or different). The mean value, width and shape of distance distributions, as well as their dependence upon the state of the protein or interactions with physiological partners, provide insight into order-disorder transitions and the roles of protein flexibility. The main potentialities and limitations of the technique are revised and illustrated with examples of proteins for which order-disorder play an important role.
000131536 536__ $$9info:eu-repo/grantAgreement/ES/DGA/E35-17R$$9info:eu-repo/grantAgreement/ES/MINECO/CTQ2015-64486-R
000131536 540__ $$9info:eu-repo/semantics/openAccess$$aby-nc-nd$$uhttp://creativecommons.org/licenses/by-nc-nd/3.0/es/
000131536 590__ $$a4.013$$b2020
000131536 591__ $$aBIOPHYSICS$$b20 / 71 = 0.282$$c2020$$dQ2$$eT1
000131536 591__ $$aBIOCHEMISTRY & MOLECULAR BIOLOGY$$b136 / 296 = 0.459$$c2020$$dQ2$$eT2
000131536 592__ $$a1.097$$b2020
000131536 593__ $$aBiochemistry$$c2020$$dQ1
000131536 593__ $$aMolecular Biology$$c2020$$dQ1
000131536 593__ $$aBiophysics$$c2020$$dQ1
000131536 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/acceptedVersion
000131536 7102_ $$12003$$2395$$aUniversidad de Zaragoza$$bDpto. Física Materia Condensa.$$cÁrea Física Materia Condensada
000131536 773__ $$g684 (2020), 108323 [14 pp.]$$pArch. biochem. biophys.$$tARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS$$x0003-9861
000131536 8564_ $$s8245186$$uhttps://zaguan.unizar.es/record/131536/files/texto_completo.pdf$$yPostprint
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000131536 951__ $$a2024-02-12-13:54:24
000131536 980__ $$aARTICLE