Atomistic modeling of a KRT35/KRT85 keratin dimer: folding in aqueous solution and unfolding under tensile load

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Details zur Publikation

Autor(en): Duchstein P, Clark T, Zahn D
Zeitschrift: Physical Chemistry Chemical Physics
Verlag: Royal Society of Chemistry
Jahr der Veröffentlichung: 2015
Band: 17
Heftnummer: 34
Seitenbereich: 21880-21884
ISSN: 1463-9076
eISSN: 1463-9084


Abstract


We present an atomistic model of a full KRT35/KRT85 dimer, a fundamental building block of human hair. For both monomers initial structures were generated using empirical tools based on homology considerations, followed by the formulation of a naive dimer model from docking the monomers in vacuum. Relaxation in aqueous solution was then explored from molecular dynamics simulation. Driven by hydrophobic segregation and protein-protein hydrogen bonding relaxation dynamics result in a folded dimer arrangement which shows a striking encounter of cystein groups. Our simulations hence suggests that (i) cystein groups in the coil regions of keratin are well suited to establish disulfide bonds between the two monomers that constitute the dimer, and (ii) the particularly large number of cystein groups in the head and tail regions promotes the connection of dimers to establish meso- to macroscale fibers. Moreover, we show the molecular mechanisms of elastic and plastic deformation under tensile load. Upon elongation beyond the elastic regime, unfolding was identified as the exposure of hydrophobic moieties and the breaking of protein-protein hydrogen bonds. Therein, the step-wise character of the series of unfolding events leads to a broad regime of constant force in response to further elongation.



FAU-Autoren / FAU-Herausgeber

Clark, Timothy apl. Prof. Dr.
Computer-Chemie-Centrum
Duchstein, Patrick Dr.
Professur für Theoretische Chemie
Zahn, Dirk Prof. Dr.
Professur für Theoretische Chemie


Zitierweisen

APA:
Duchstein, P., Clark, T., & Zahn, D. (2015). Atomistic modeling of a KRT35/KRT85 keratin dimer: folding in aqueous solution and unfolding under tensile load. Physical Chemistry Chemical Physics, 17(34), 21880-21884. https://dx.doi.org/10.1039/c5cp02676h

MLA:
Duchstein, Patrick, Timothy Clark, and Dirk Zahn. "Atomistic modeling of a KRT35/KRT85 keratin dimer: folding in aqueous solution and unfolding under tensile load." Physical Chemistry Chemical Physics 17.34 (2015): 21880-21884.

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Zuletzt aktualisiert 2018-07-08 um 04:52