Statistical mechanics of protein-like heteropolymers.
نویسندگان
چکیده
A strategy is outlined for obtaining the free energy of a typical designed heteropolymer. The design procedure considers the probability that the target conformation is occupied in comparison with all the other conformations that could house the given sequence. Numerical calculations on lattice heteropolymer models are presented to illustrate the key physical principles.
منابع مشابه
Theory of protein folding: the energy landscape perspective.
The energy landscape theory of protein folding is a statistical description of a protein's potential surface. It assumes that folding occurs through organizing an ensemble of structures rather than through only a few uniquely defined structural intermediates. It suggests that the most realistic model of a protein is a minimally frustrated heteropolymer with a rugged funnel-like landscape biased...
متن کاملConformational transitions of heteropolymers
We study conformational transitions of simple coarse-grained models for protein-like heteropolymers on the simple cubic lattice and off-lattice, respectively, by means of multicanonical sampling algorithms. The effective hydrophobic/polar models do not require the knowledge of the native topology for a given sequence of residues as input. Therefore these models are eligible to investigate gener...
متن کاملStatistical mechanics of a correlated energy landscape model for protein folding funnels
In heteropolymers, energetic correlations exist due to polymeric constraints and the locality of interactions. Pair correlations in conjunction with the a priori specification of the existence of a particularly low energy state provide a method of introducing the aspect of minimal frustration to the energy landscapes of random heteropolymers. The resulting funneled landscape exhibits both a pha...
متن کاملStatistical mechanics of correlated energy landscape models for random heteropolymers and proteins
We study the role of correlations in the energy landscape of heteropolymers and proteins, specifically their role in the glass transition in random heteropolymers and the folding transition in minimally frustrated proteins. In the context of the glass transition, a correlated landscape results in a more gradual freezing into basins of extensive entropy, while not completely destroying the first...
متن کاملReversible stretching of random heteropolymers.
We analyze the equilibrium response of random heteropolymers to mechanical deformation. In contrast to homopolymer response, the stress-induced transformation of a heteropolymer from globule to coil need not be sharp. For chain lengths relevant to biological macromolecules, intermediate necklace-like structures dominate over a range of applied force. Stability of these conformations is primaril...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- Proceedings of the National Academy of Sciences of the United States of America
دوره 96 9 شماره
صفحات -
تاریخ انتشار 1999