Proteins top-down: a statistical mechanics approach

Citation
A. Hansen et al., Proteins top-down: a statistical mechanics approach, PHYSICA A, 288(1-4), 2000, pp. 21-30
Citations number
11
Categorie Soggetti
Physics
Journal title
PHYSICA A
ISSN journal
03784371 → ACNP
Volume
288
Issue
1-4
Year of publication
2000
Pages
21 - 30
Database
ISI
SICI code
0378-4371(200012)288:1-4<21:PTASMA>2.0.ZU;2-S
Abstract
Biopolymers have many fascinating properties coming from a competition betw een universal features, well known in the physics of synthetic polymers, an d specific elements which are crucial for the biological function of these molecules. Proteins are an example of this richness: proteins are heteropol ymers consisting of hydrophobic and hydrophilic segments, and carry charges of both signs along the backbone. Simple models of such heteropolymers hav e been studied in connection with the folding and evolution of proteins. Ho wever, these models can only give a limited understanding of real proteins, and elements specific to proteins must be included. Our approach to this p roblem has been to construct a model of the specific self-interactions of p roteins by defining a unique folding pathway. This model reproduces the the rmodynamic properties of proteins. (C) 2000 Elsevier Science B.V. All right s reserved.