Cooperativity of Protein Folding and the Random-Field Ising Model
A. M. Gutin, V. I. Abkevich, E. I. Shakhnovich
Abstract
The relation between cooperativity of protein folding and the Random-Field Ising Model (RFIM) is established. Generalization of the Imry-Ma argument predicts cooperative folding transition for small heterogeneity of the interactions stabilizing the native structure. Monte Carlo simulation of a lattice model shows that starting from some finite heterogeneity folding transition is not cooperative and involves formation of domains.
Create a lesson
Related papers
Knots in Condensed Matters
Y. M. Cho
Bouchaud's model exhibits two different aging regimes in dimension one
Gerard Ben Arous, Jiri Cerny
Periodic diffraction patterns for 1D quasicrystals
Pawel Buczek, Lorenzo Sadun, Janusz Wolny
Adiabatic association of ultracold molecules via magnetic field tunable interactions
Krzysztof Goral, Thorsten Koehler, Simon A. Gardiner et al.
High-Temperature Atomic Superfluidity in Lattice Boson-Fermion Mixtures
F. Illuminati, A. Albus
Constructive Methods of Invariant Manifolds for Kinetic Problems
A. N. Gorban, I. V. Karlin, A. Yu. Zinovyev