Relaxation kinetics and the glassiness of proteins: the case of bovine pancreatic trypsin inhibitor

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Baysal, Canan and Atılgan, Ali Rana (2002) Relaxation kinetics and the glassiness of proteins: the case of bovine pancreatic trypsin inhibitor. Biophysical Journal, 83 (2). pp. 699-705. ISSN 0006-3495 (Print) 1542-0086 (Online)

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Abstract

Folded proteins may be regarded as soft active matter under physiological conditions. The densely packed hydrophobic interior, the relatively molten hydrophilic exterior, and the spacer connecting these put together a large number of locally homogenous regions. For the case of the bovine pancreatic trypsin inhibitor, with the aid of molecular dynamics simulations, we have demonstrated that the kinetics of the relaxation of the internal motions is highly concerted, manifesting the protein's heterogeneity, which may arise from variations in density, local packing, or the local energy landscape. This behavior is characterized in a stretched exponential decay described by an exponent of similar to0.4 at physiological temperatures. Due to the trapped conformations, configurational entropy becomes smaller, and the associated stretch exponent drops to half of its value below the glass transition range. The temperature dependence of the inverse relaxation time closely follows the Vogel-Tamman-Fulcher expression when the protein is biologically active.
Item Type: Article
Additional Information: WoS - Open Access (Green Published, Bronze) / Scopus - Open Access
Divisions: Faculty of Engineering and Natural Sciences > Academic programs > Materials Science & Eng.
Faculty of Engineering and Natural Sciences
Depositing User: Canan Atılgan
Date Deposited: 17 Jun 2020 15:03
Last Modified: 26 Apr 2022 10:15
URI: https://research.sabanciuniv.edu/id/eprint/39967

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