Mean-Field HP Model, Designability and Alpha-Helices in Protein Structures
C. T. Shih, Z. Y. Su, J. F. Gwan, H. C. Lee, B. L. Hao, C. H. Hsieh
Abstract
Analysis of the geometric properties of a mean-field HP model on a square lattice for protein structure shows that structures with large number of switch backs between surface and core sites are chosen favorably by peptides as unique ground states. Global comparison of model (binary) peptide sequences with concatenated (binary) protein sequences listed in the Protein Data Bank and the Dali Domain Dictionary indicates that the highest correlation occurs between model peptides choosing the favored structures and those portions of protein sequences containing alpha-helices.
Create a lesson
Related papers
Nonparametric multiscale modeling of boundary lubrication: hexadecane in highly pressurized gold asperity contacts
Hannes Holey, Michael Moseler, Peter Gumbsch et al.
Asymmetric Ions in Solution are Similar to Active Brownian Particles
Setare Mostajabi Sarhangi, Dmitry V. Matyushov
Influence of twist direction and large deformation on soft material torsional contact
Yucai Hu, Pengfei Li, Michele Ciavarella et al.
Phase transitions and microphases in elastomers. II. Anisotropy-driven morphologies
Manu Mannattil, David Andelman, Haim Diamant
Comparing non-local granular fluid continuum models for silo discharge: Toward clogging prediction
Y. Zhou, Y. Wang, M. Li et al.
Residual semi-crystalline particles released during enzymatic degradation of plastics
Michael Schindler, Ludwik Leibler