Phys. Rev. E 104, 034414 (2021) - Protein dynamics implications of the low- and high-temperature denaturation of myoglobin

Protein dynamics implications of the low- and high-temperature denaturation of myoglobin

Ramzi R. Khuri, Trung V. Phan, and Robert H. Austin

Phys. Rev. E 104, 034414 – Published 24 September 2021

Abstract

We reinvestigate a simple model used in the literature concerning the thermodynamic analysis of protein cold denaturation. We derive an exact thermodynamic expression for cold denaturation and give a better approximation than exists in the literature for predicting cold denaturation temperatures in the two-state model. We discuss the “dark-side” implications of this work for previous temperature-dependent protein dynamics experiments and discuss microfluidic experimental technologies, which could explore the thermal stability range of proteins below the bulk freezing point of water.

Received 31 October 2020
Revised 18 June 2021
Accepted 19 August 2021

DOI:https://doi.org/10.1103/PhysRevE.104.034414

©2021 American Physical Society

Physics Subject Headings (PhySH)

Protein structure prediction

Physics of Living Systems

Authors & Affiliations

Ramzi R. Khuri ^*

Department of Natural Sciences, Baruch College, City University of New York, New York, New York 10010, USA

Trung V. Phan ^† and Robert H. Austin ^‡

Department of Physics, Princeton University, Princeton, New Jersey 08544, USA

^*ramzi.khuri@baruch.cuny.edu
^†tvphan@princeton.edu
^‡austin@princeton.edu

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Issue

Vol. 104, Iss. 3 — September 2021

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