Premium
Minimal model for studying prion‐like folding pathways
Author(s) -
Chen Jeff Z. Y.,
Lemak Alexander S.,
Lepock James R.,
Kemp Josh P.
Publication year - 2003
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.10329
Subject(s) - folding (dsp implementation) , energy landscape , protein folding , beta sheet , beta (programming language) , alpha helix , downhill folding , chemistry , monte carlo method , helix (gastropod) , hydrogen bond , protein secondary structure , lattice protein , crystallography , chemical physics , protein structure , physics , molecule , mathematics , biology , phi value analysis , computer science , biochemistry , ecology , statistics , organic chemistry , snail , electrical engineering , programming language , engineering
The Monte Carlo technique is used to simulate the energy landscape and the folding kinetics of a minimal prion‐like protein model. We show that the competition between hydrogen‐bonding and hydrophobic interactions yields two energetically favored secondary structures, an α‐helix and a β‐hairpin. Folding simulations indicate that the probability of reaching the α‐helix form from a denatured random conformation is much higher than the probability of reaching the β‐sheet form, even though the β‐sheet has a lower energy. The existence of a lower energy β‐sheet state gives the possibility for the normal α‐helix structure to take a structural transformation into the β‐sheet structure under external influences. Proteins 2003;51:283–288. © 2003 Wiley‐Liss, Inc.