Publisher’s Note: “Coupled folding–binding versus docking: A lattice model study” [J. Chem. Phys. 120, 3983 (2004)]

2004 ◽  
Vol 120 (18) ◽  
pp. 8871-8871
Author(s):  
Nitin Gupta ◽  
Anders Irbäck
Keyword(s):  
Lattice Model ◽  
Chem Phys ◽  
Model Study

scholarly journals Active and passive transport of cargo in a corrugated channel: A lattice model study

2018 ◽  
Vol 148 (13) ◽  
pp. 134907 ◽  
Author(s):  
Supravat Dey ◽  
Kevin Ching ◽  
Moumita Das
Keyword(s):  
Lattice Model ◽  
Passive Transport ◽  
Corrugated Channel ◽  
Model Study

The role of cotranslation in protein folding: a lattice model study

Polymer ◽  
2004 ◽  
Vol 45 (2) ◽  
pp. 557-571 ◽  
Author(s):  
M.P. Morrissey ◽  
Z. Ahmed ◽  
E.I. Shakhnovich
Keyword(s):  
Protein Folding ◽  
Lattice Model ◽  
Model Study

Protein translocation through a tunnel induces changes in folding kinetics: A lattice model study

2006 ◽  
Vol 94 (1) ◽  
pp. 105-117 ◽  
Author(s):  
Lydia M. Contreras Martínez ◽  
Francisco J. Martínez-Veracoechea ◽  
Prabhas Pohkarel ◽  
Abraham D. Stroock ◽  
Fernando A. Escobedo ◽  
...  
Keyword(s):  
Lattice Model ◽  
Protein Translocation ◽  
Folding Kinetics ◽  
Model Study

scholarly journals Deriving amino acid contact potentials from their frequencies of occurrence in proteins: a lattice model study

2004 ◽  
Vol 16 (15) ◽  
pp. 2551-2564 ◽  
Author(s):  
G Tiana ◽  
M Colombo ◽  
D Provasi ◽  
R A Broglia
Keyword(s):  
Amino Acid ◽  
Lattice Model ◽  
Model Study

scholarly journals SELECTIVE ADVANTAGE OF RECOMBINATION IN EVOLVING PROTEIN POPULATIONS: A LATTICE MODEL STUDY

2006 ◽  
Vol 17 (01) ◽  
pp. 75-90 ◽  
Author(s):  
PAUL D. WILLIAMS ◽  
DAVID D. POLLOCK ◽  
RICHARD A. GOLDSTEIN
Keyword(s):  
Homologous Recombination ◽  
Lattice Model ◽  
Selective Advantage ◽  
Native Structure ◽  
Fitness Level ◽  
Model Study ◽  
Protein Model ◽  
Evolutionary Advantage ◽  
Protein Models ◽  
Mutational Processes

Recent research has attempted to clarify the contributions of several mutational processes, such as substitutions or homologous recombination. Simplistic, tractable protein models, which determine the compact native structure phenotype from the sequence genotype, are well-suited to such studies. In this paper, we use a lattice-protein model to examine the effects of point mutation and homologous recombination on evolving populations of proteins. We find that while the majority of mutation and recombination events are neutral or deleterious, recombination is far more likely to be beneficial. This results in a faster increase in fitness during evolution, although the final fitness level is not significantly changed. This transient advantage provides an evolutionary advantage to subpopulations that undergo recombination, allowing fixation of recombination to occur in the population.

An Analytical Lattice Model Study of fcc Nanowires

2008 ◽  
Vol 5 (3) ◽  
pp. 341-347 ◽  
Author(s):  
I-Ling Chang ◽  
Jen-Chin Huang
Keyword(s):  
Lattice Model ◽  
Model Study

scholarly journals Lattice Model Study of Proteins with Orientation-dependent Interactions

1999 ◽  
Vol 39 (supplement) ◽  
pp. S167
Author(s):  
T. P. Terada ◽  
M. Sasai
Keyword(s):  
Lattice Model ◽  
Model Study

scholarly journals Lattice-model study of the thermodynamic interplay of polymer crystallization and liquid–liquid demixing

2003 ◽  
Vol 118 (22) ◽  
pp. 10343-10348 ◽  
Author(s):  
Wenbing Hu ◽  
Daan Frenkel ◽  
Vincent B. F. Mathot
Keyword(s):  
Lattice Model ◽  
Polymer Crystallization ◽  
Model Study
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