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The Finite Size Effects and Two-State Paradigm of Protein Folding

Materials Research Laboratory, University of Nova Gorica, Vipavska 13, SI-5000 Nova Gorica, Slovenia
Institute of Fundamental and Frontier Sciences, University of Electronic Science and Technology of China, Chengdu 610054, China
National Institute of Chemistry, Hajdrihova 19, SI-1000 Ljubljana, Slovenia
Department of Molecular Medicine, USF Health Byrd Alzheimer’s Research Institute, Morsani College of Medicine, University of South Florida, 12901 Bruce B. Downs Blvd., MDC07, Tampa, FL 33612, USA
Author to whom correspondence should be addressed.
Academic Editor: Shin-ichi Tate
Int. J. Mol. Sci. 2021, 22(4), 2184;
Received: 27 January 2021 / Revised: 10 February 2021 / Accepted: 15 February 2021 / Published: 22 February 2021
(This article belongs to the Special Issue Protein Structure Dynamics and Function)
The coil to globule transition of the polypeptide chain is the physical phenomenon behind the folding of globular proteins. Globular proteins with a single domain usually consist of about 30 to 100 amino acid residues, and this finite size extends the transition interval of the coil-globule phase transition. Based on the pedantic derivation of the two-state model, we introduce the number of amino acid residues of a polypeptide chain as a parameter in the expressions for two cooperativity measures and reveal their physical significance. We conclude that the k2 measure, defined as the ratio of van ’t Hoff and calorimetric enthalpy is related to the degeneracy of the denatured state and describes the number of cooperative units involved in the transition; additionally, it is found that the widely discussed k2=1 is just the necessary condition to classify the protein as the two-state folder. We also find that Ωc, a quantity not limited from above and growing with system size, is simply proportional to the square of the transition interval. This fact allows us to perform the classical size scaling analysis of the coil-globule phase transition. Moreover, these two measures are shown to describe different characteristics of protein folding. View Full-Text
Keywords: protein folding; two-state model; size scaling; thermodynamic cooperativity protein folding; two-state model; size scaling; thermodynamic cooperativity
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MDPI and ACS Style

Badasyan, A.; Valant, M.; Grdadolnik, J.; Uversky, V.N. The Finite Size Effects and Two-State Paradigm of Protein Folding. Int. J. Mol. Sci. 2021, 22, 2184.

AMA Style

Badasyan A, Valant M, Grdadolnik J, Uversky VN. The Finite Size Effects and Two-State Paradigm of Protein Folding. International Journal of Molecular Sciences. 2021; 22(4):2184.

Chicago/Turabian Style

Badasyan, Artem, Matjaz Valant, Jože Grdadolnik, and Vladimir N. Uversky. 2021. "The Finite Size Effects and Two-State Paradigm of Protein Folding" International Journal of Molecular Sciences 22, no. 4: 2184.

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