Quasiequilibrium unfolding thermodynamics of a small protein studied by molecular dynamics simulation with an explicit water model

The 124 independent molecular dynamics simulations are completed with total time of 196.8 ns. The calculated unfolding quasiequilibrium thermodynamics of G-IgG-binding domain B1 (GB1) shows the experimentally observed protein transitions: a coil to disordered globule transition, a disordered globule...

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Bibliographic Details
Published in:Physical review. E, Statistical, nonlinear, and soft matter physics Statistical, nonlinear, and soft matter physics, 2003-06, Vol.67 (6 Pt 1), p.061903-061903
Main Authors: Wang, Jihua, Zhang, Zhiyong, Liu, Haiyan, Shi, Yunyu
Format: Article
Language:English
Subjects:
Bacterial Proteins - chemistry
Computer Simulation
Hot Temperature
Immunoglobulin G - chemistry
Models, Molecular
Models, Statistical
Pressure
Protein Binding
Protein Conformation
Protein Denaturation
Protein Folding
Protein Structure, Secondary
Protein Structure, Tertiary
Proteins - chemistry
Temperature
Thermodynamics
Time Factors
Water - chemistry
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Summary:The 124 independent molecular dynamics simulations are completed with total time of 196.8 ns. The calculated unfolding quasiequilibrium thermodynamics of G-IgG-binding domain B1 (GB1) shows the experimentally observed protein transitions: a coil to disordered globule transition, a disordered globule to molten globule transition, a molten globule to nativelike transition, and a nativelike to solidlike state transition. The first protein unfolding phase diagram has been constructed from molecular dynamics simulations with an explicit water model. The calculated melting temperature of GB1 agrees with early experiment. The results also agree with the recent experiment result in which GB1 has more than one intermediate.
ISSN:1539-3755
DOI:10.1103/PhysRevE.67.061903