000063273 001__ 63273
000063273 005__ 20171129112116.0
000063273 0247_ $$2doi$$a10.1371/journal.pcbi.1002647
000063273 0248_ $$2sideral$$a78974
000063273 037__ $$aART-2012-78974
000063273 041__ $$aeng
000063273 100__ $$aGarcía-Fandiño, R.
000063273 245__ $$aDefining the Nature of Thermal Intermediate in 3 State Folding Proteins: Apoflavodoxin, a Study Case
000063273 260__ $$c2012
000063273 5060_ $$aAccess copy available to the general public$$fUnrestricted
000063273 5203_ $$aThe early stages of the thermal unfolding of apoflavodoxin have been determined by using atomistic multi microsecond-scale molecular dynamics (MD) simulations complemented with a variety of experimental techniques. Results strongly suggest that the intermediate is reached very early in the thermal unfolding process and that it has the properties of an “activated” form of the native state, where thermal fluctuations in the loops break loop-loop contacts. The unrestrained loops gain then kinetic energy corrupting short secondary structure elements without corrupting the core of the protein. The MD-derived ensembles agree with experimental observables and draw a picture of the intermediate state inconsistent with a well-defined structure and characteristic of a typical partially disordered protein. Our results allow us to speculate that proteins with a well packed core connected by long loops might behave as partially disordered proteins under native conditions, or alternatively behave as three state folders. Small details in the sequence, easily tunable by evolution, can yield to one or the other type of proteins.
000063273 536__ $$9info:eu-repo/grantAgreement/ES/DGA/B89$$9info:eu-repo/grantAgreement/ES/MICINN/BFU2010-16296$$9info:eu-repo/grantAgreement/ES/MICINN/BIO2009-10964
000063273 540__ $$9info:eu-repo/semantics/openAccess$$aby$$uhttp://creativecommons.org/licenses/by/3.0/es/
000063273 590__ $$a4.867$$b2012
000063273 591__ $$aMATHEMATICAL & COMPUTATIONAL BIOLOGY$$b4 / 47 = 0.085$$c2012$$dQ1$$eT1
000063273 591__ $$aBIOCHEMICAL RESEARCH METHODS$$b11 / 74 = 0.149$$c2012$$dQ1$$eT1
000063273 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/publishedVersion
000063273 700__ $$aBernadó, P.
000063273 700__ $$aAyuso-Tejedor, S.
000063273 700__ $$0(orcid)0000-0002-2879-9200$$aSancho, J.$$uUniversidad de Zaragoza
000063273 700__ $$aOrozco, M.
000063273 7102_ $$11002$$2060$$aUniversidad de Zaragoza$$bDepartamento de Bioquímica y Biología Molecular y Celular$$cBioquímica y Biología Molecular
000063273 773__ $$g8, 8 (2012), e10026 [15 pp]$$pPLoS Comput. Biol.$$tPLoS Computational Biology$$x1553-734X
000063273 8564_ $$s1787310$$uhttps://zaguan.unizar.es/record/63273/files/texto_completo.pdf$$yVersión publicada
000063273 8564_ $$s130729$$uhttps://zaguan.unizar.es/record/63273/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada
000063273 909CO $$ooai:zaguan.unizar.es:63273$$particulos$$pdriver
000063273 951__ $$a2017-11-28-12:44:58
000063273 980__ $$aARTICLE