Heterogeneous dynamics in partially disordered proteins

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dc.contributor.author Virtanen, Salla
dc.contributor.author Kiirikki, Anne M.
dc.contributor.author Mikula, Kornelia M.
dc.contributor.author Iwai, Hideo
dc.contributor.author Ollila, O. H. Samuli
dc.date.accessioned 2021-06-10T12:28:01Z
dc.date.available 2021-06-10T12:28:01Z
dc.date.issued 2020-10-07
dc.identifier.citation Virtanen , S , Kiirikki , A M , Mikula , K M , Iwai , H & Ollila , O H S 2020 , ' Heterogeneous dynamics in partially disordered proteins ' , Physical Chemistry Chemical Physics , vol. 22 , no. 37 , pp. 21185-21196 . https://doi.org/10.1039/d0cp03473h
dc.identifier.other PURE: 157735267
dc.identifier.other PURE UUID: da991bce-6e4e-449f-a518-ee4fcc1a7b18
dc.identifier.other WOS: 000573875300020
dc.identifier.other ORCID: /0000-0001-7376-5264/work/85516930
dc.identifier.uri http://hdl.handle.net/10138/330837
dc.description.abstract Importance of disordered protein regions is increasingly recognized in biology, but their characterization remains challenging due to the lack of suitable experimental and theoretical methods. NMR experiments can detect multiple timescale dynamics and structural details of disordered protein regions, but their detailed interpretation is often difficult. Here we combine protein backbone(15)N spin relaxation data with molecular dynamics (MD) simulations to detect not only heterogeneous dynamics of large partially disordered proteins but also their conformational ensembles. We observed that the rotational dynamics of folded regions in partially disordered proteins is dominated by similar rigid body rotation as in globular proteins, thereby being largely independent of flexible disordered linkers. Disordered regions, on the other hand, exhibit complex rotational motions with multiple timescales below similar to 30 ns which are difficult to detect from experimental data alone, but can be captured by MD simulations. Combining MD simulations and backbone(15)N spin relaxation data, measured applying segmental isotopic labeling with salt-inducible split intein, we resolved the conformational ensemble and dynamics of partially disordered periplasmic domain of TonB protein fromHelicobacter pyloricontaining 250 residues. To demonstrate the universality of our approach, it was applied also to the partially disordered region of chicken Engrailed 2. Our results pave the way in understanding how TonB transfers energy from inner membrane to the outer membrane receptors in Gram-negative bacteria, as well as the function of other proteins with disordered domains. en
dc.format.extent 12
dc.language.iso eng
dc.relation.ispartof Physical Chemistry Chemical Physics
dc.rights cc_by
dc.rights.uri info:eu-repo/semantics/openAccess
dc.subject NMR-SPECTROSCOPY
dc.subject BACKBONE DYNAMICS
dc.subject ESCHERICHIA-COLI
dc.subject CONFORMATIONAL DYNAMICS
dc.subject N-15 RELAXATION
dc.subject FORCE-FIELD
dc.subject TONB
dc.subject DOMAIN
dc.subject MODEL
dc.subject PREDICTION
dc.subject 114 Physical sciences
dc.subject 116 Chemical sciences
dc.title Heterogeneous dynamics in partially disordered proteins en
dc.type Article
dc.contributor.organization Biochemistry and Biotechnology
dc.contributor.organization Institute of Biotechnology
dc.contributor.organization Hideo Iwai / Principal Investigator
dc.contributor.organization Doctoral Programme in Drug Research
dc.contributor.organization Biophysical chemistry
dc.description.reviewstatus Peer reviewed
dc.relation.doi https://doi.org/10.1039/d0cp03473h
dc.relation.issn 1463-9076
dc.rights.accesslevel openAccess
dc.type.version publishedVersion

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