Electrostatic contributions to T4 lysozyme stability: solvent-exposed charges versus semi-buried salt bridges.

doi:10.1016/S0006-3495(02)73904-0

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Article

Electrostatic contributions to T4 lysozyme stability: solvent-exposed charges versus semi-buried salt bridges.

Biophysical journal - 1 Sept 2002

Dong Feng, Zhou Huan-Xiang

Abstract excerpt

We carried our Poisson-Boltzmann (PB) calculations for the effects of charge reversal at five exposed sites (K16E, R119E, K135E, K147E, and R154E) and charge neutralization and proton titration of the H31-D70 semi-buried salt bridge on the stability of T4 lysozyme. Instead of the widely used solvent-exclusion (SE) surface, we used the van der Waals (vdW) surface as the boundary between the protein and solvent...

Topics

Bacillus subtilis
Bacteriophage T4
Hydrogen-Ion Concentration
Models, Molecular
Muramidase
Mutation
Protein Folding
Salts
Solvents
Static Electricity
Thermodynamics

Source

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Identifiers

PMID: 12202359
DOI: 10.1016/S0006-3495(02)73904-0
PMCID: PMC1302232

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