TY - JOUR
T1 - Glassy Dynamics of Side-Chain Ordering in a Simple Model of Protein Folding
AU - Kussell, Edo
AU - Shakhnovich, Eugene I.
N1 - Funding Information:
This work was supported by NIH Grant No. RO1-52126. We thank J. Shimada, W. Chen, and G. Berriz for interesting discussions and L. Mirny for providing fast-folding sequences.
PY - 2002
Y1 - 2002
N2 - We introduce a modified version of protein lattice models in which monomers have several spin states, representing side-chain rotamers. Completion of folding corresponds to reaching the native backbone configuration with complete ordering of side chains. We find that as temperature is lowered, side-chain ordering becomes much slower than backbone folding. The presence of side chains leads to nonexponential kinetics and a broad distribution of relaxation times.
AB - We introduce a modified version of protein lattice models in which monomers have several spin states, representing side-chain rotamers. Completion of folding corresponds to reaching the native backbone configuration with complete ordering of side chains. We find that as temperature is lowered, side-chain ordering becomes much slower than backbone folding. The presence of side chains leads to nonexponential kinetics and a broad distribution of relaxation times.
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U2 - 10.1103/PhysRevLett.89.168101
DO - 10.1103/PhysRevLett.89.168101
M3 - Article
C2 - 12398757
AN - SCOPUS:18744414792
SN - 0031-9007
VL - 89
JO - Physical Review Letters
JF - Physical Review Letters
IS - 16
ER -