The Origin of the Designability of Protein Structures
Rie Tatsumi, George Chikenji
Abstract
We examined what determines the designability of 2-letter codes (H and P) lattice proteins from three points of view. First, whether the native structure is searched within all possible structures or within maximally compact structures. Second, whether the structure of the used lattice is bipartite or not. Third, the effect of the length of the chain, namely, the number of monomers on the chain. We found that the bipartiteness of the lattice structure is not a main factor which determines the designability. Our results suggest that highly designable structures will be found when the length of the chain is sufficiently long to make the hydrophobic core consisting of enough number of monomers.
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