Special Issue "Entropies of Polymers"

Guest Editor
Dr. Donald J. Jacobs
Department of Physics and Optical Science, University of North Carolina at Charlotte, 9201 University City Blvd., Charlotte, NC 28223, USA
Website: http://maxwell.uncc.edu/djacobs1/
E-Mail:
Interests: computational physics; biological physics; protein stability; phase transitions; brownian motion

Related Special Issues in other Journals

Entropies of Polymers in Polymers

Submission

All papers should be submitted to entropy@mdpi.org with copy to the guest editor. To be published continuously until the deadline and papers will be listed together at the special websites. Both, research articles and review articles are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editors for announcment on this website.

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Please visit the Instructions for Authors page before submitting a paper. Open Access publication fees are 800 CHF per paper. English correction fees (250 CHF) will be added in certain cases (1050 CHF per paper for those papers that require extensive additional formatting and/or English corrections.).

List of Related Papers

See a list of related papers on configurational entropy compiled by Shu-Kun Lin

• computational physics
• biological physics
• protein stability
• phase transitions
• Brownian motion

Type of Paper: Review
Title: Eye Lens Proteins: The Energetics of Homo and Hetero-Association of the βγ-Crystallins
Authors: Yuri V. Sergeev ¹, M. Dolinska ¹ and P.T. Wingfield ²
Affiliations: ¹ National Eye Institute, National Institutes of Health, Bethesda, Maryland, USA; E-Mail: SergeevY@NEI.NIH.GOV
² National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland, USA
Abstract: β-Crystallins are the major protein components of the eye lens and have conserved structures which include: N- and C-terminal extensions of variable length and of unknown function, and two β-structural globular domains with a high sequence similarity within a protein family. The association of these proteins into stable higher order homo- and hetero-associates is critical for lens clarity and refraction and overall defines the quality of human vision. Lens protein stability is compromised by pathogenic mutations, ageing processes and other factors, which enhance association of βA3-, βB1- and βB2-crystallins resulting in insoluble protein formation and cataract. To understand the energetics of the interactions of wild type and modified crystallins various experimentation and computational approaches can be applied. All three β-crystallins demonstrate fast reversible monomer-dimer equilibria with a tendency to form tighter dimers at higher temperatures; this suggests entropic control mediated by hydrophobic interactions. Further detail from modeling indicates that monomeric protein is in rapid equilibrium between two conformational states prior to dimer association. In contrast, hetero-molecular crystallin associations, best described as hetero-dimer – tetramer system, appear to be controlled by enthalpy effects and indicates involvement of Van-der-Waals and polar forces at the interaction surface.