Abstract

We performed molecular dynamics simulations of the collapse of a two-domain protein, the BphC enzyme, into a globular structure to examine how water molecules mediate hydrophobic collapse of proteins. In the interdomain region, liquid water persists with a density 10to 15% lower than in the bulk, even at small domain separations. Water depletion and hydrophobic collapse occur on a nanosecond time scale, which is two orders of magnitude slower than that found in the collapse of idealized paraffin-like plates. When the electrostatic protein-water forces are turned off, a dewetting transition occurs in the interdomain region and the collapse speeds up by more than an order of magnitude. When attractive van der Waals forces are turned off as well, the dewetting in the interdomain region is more profound, and the collapse is even faster.

Keywords

DewettingChemical physicsvan der Waals forceProtein foldingFolding (DSP implementation)ChemistryGlobular proteinMolecular dynamicsCrystallographyMoleculePhysicsWettingThermodynamicsComputational chemistry

Affiliated Institutions

Related Publications

Publication Info

Year
2004
Type
article
Volume
305
Issue
5690
Pages
1605-1609
Citations
510
Access
Closed

External Links

View on DOI.org

Social Impact

Altmetric
PlumX Metrics

Social media, news, blog, policy document mentions

Citation Metrics

510
OpenAlex

Cite This

Ruhong Zhou, Xuhui Huang, Claudio J. Margulis et al. (2004). Hydrophobic Collapse in Multidomain Protein Folding. Science , 305 (5690) , 1605-1609. https://doi.org/10.1126/science.1101176

Identifiers

DOI
10.1126/science.1101176