Molecular dynamics simulations of the hydrophobin SC3 at a hydrophobic/hydrophilic interface

Fan, Hao, Wang, Xiaoqin, Zhu, Jiang, Robillard, George T. and Mark, Alan E. (2006) Molecular dynamics simulations of the hydrophobin SC3 at a hydrophobic/hydrophilic interface. Proteins-structure Function And Bioinformatics, 64 4: 863-873. doi:10.1002/prot.20936

Author Fan, Hao
Wang, Xiaoqin
Zhu, Jiang
Robillard, George T.
Mark, Alan E.
Title Molecular dynamics simulations of the hydrophobin SC3 at a hydrophobic/hydrophilic interface
Journal name Proteins-structure Function And Bioinformatics   Check publisher's open access policy
ISSN 0887-3585
Publication date 2006-01-01
Year available 2006
Sub-type Article (original research)
DOI 10.1002/prot.20936
Open Access Status
Volume 64
Issue 4
Start page 863
End page 873
Total pages 11
Place of publication Hoboken
Publisher Wiley-Liss
Language eng
Subject C1
060112 Structural Biology (incl. Macromolecular Modelling)
030799 Theoretical and Computational Chemistry not elsewhere classified
Abstract Hydrophobins are small (similar to 100 aa) proteins that have an important role in the growth and development of mycelial fungi. They are surface active and, after secretion by the fungi, self-assemble into amphipathic membranes at hydrophobic/hydrophilic interfaces, reversing the hydrophobicity of the surface. In this study, molecular dynamics simulation techniques have been used to model the process by which a specific class I hydrophobin, SC3, binds to a range of hydrophobic/ hydrophilic interfaces. The structure of SC3 used in this investigation was modeled based on the crystal structure of the class II hydrophobin HFBII using the assumption that the disulfide pairings of the eight conserved cysteine residues are maintained. The proposed model for SC3 in aqueous solution is compact and globular containing primarily P-strand and coil structures. The behavior of this model of SC3 was investigated at an air/water, an oil/water, and a hydrophobic solid/water interface. It was found that SC3 preferentially binds to the interfaces via the loop region between the third and fourth cysteine residues and that binding is associated with an increase in a-helix formation in qualitative agreement with experiment. Based on a combination of the available experiment data and the current simulation studies, we propose a possible model for SC3 self-assembly on a hydrophobic solid/water interface.
Keyword Hydrophobin
Structure Prediction
Molecular Dynamics
Biochemistry & Molecular Biology
Protein Secondary Structure
Atom Force-field
Fungal Hydrophobin
Fold Recognition
Fruiting Bodies
Q-Index Code C1
Institutional Status UQ

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Created: Wed, 15 Aug 2007, 18:59:40 EST