The Finite Size Effects and Two-State Paradigm of Protein Folding
1
Materials Research Laboratory, University of Nova Gorica, Vipavska 13, SI-5000 Nova Gorica, Slovenia
2
Institute of Fundamental and Frontier Sciences, University of Electronic Science and Technology of China, Chengdu 610054, China
3
National Institute of Chemistry, Hajdrihova 19, SI-1000 Ljubljana, Slovenia
4
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; https://doi.org/10.3390/ijms22042184
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 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 is just the necessary condition to classify the protein as the two-state folder. We also find that , 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.
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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. https://doi.org/10.3390/ijms22042184
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. https://doi.org/10.3390/ijms22042184
Chicago/Turabian StyleBadasyan, Artem; Valant, Matjaz; Grdadolnik, Jože; Uversky, Vladimir N. 2021. "The Finite Size Effects and Two-State Paradigm of Protein Folding" Int. J. Mol. Sci. 22, no. 4: 2184. https://doi.org/10.3390/ijms22042184
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