help button home button Biophys. J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Zangi, R.
Right arrow Articles by Mark, A. E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Zangi, R.
Right arrow Articles by Mark, A. E.

Biophys J, July 2002, p. 112-124, Vol. 83, No. 1

Molecular Dynamics Study of the Folding of Hydrophobin SC3 at a Hydrophilic/Hydrophobic Interface

Ronen Zangi,* Marcel L. de Vocht,dagger George T. Robillard,dagger Dagger and Alan E. Mark*

 *Department of Biophysical Chemistry and  dagger Department of Biochemistry, University of Groningen, and  Dagger Biomade Technology Foundation, Nijenborgh 4, 9747 AG Groningen, The Netherlands

Hydrophobins are fungal proteins that self-assemble at hydrophilic/hydrophobic interfaces into amphipathic membranes. These assemblages are extremely stable and posses the remarkable ability to invert the polarity of the surface on which they are adsorbed. Neither the three-dimensional structure of a hydrophobin nor the mechanism by which they function is known. Nevertheless, there are experimental indications that the self-assembled form of the hydrophobins SC3 and EAS at a water/air interface is rich with beta -sheet secondary structure. In this paper we report results from molecular dynamics simulations, showing that fully extended SC3 undergoes fast (~100 ns) folding at a water/hexane interface to an elongated planar structure with extensive beta -sheet secondary elements. Simulations in each of the bulk solvents result in a mainly unstructured globular protein. The dramatic enhancement in secondary structure, whether kinetic or thermodynamic in origin, highlights the role interfaces between phases with large differences in polarity can have on folding. The partitioning of the residue side-chains to one of the two phases can serve as a strong driving force to initiate secondary structure formation. The interactions of the side-chains with the environment at an interface can also stabilize configurations that otherwise would not occur in a homogenous solution.

Biophys J, July 2002, p. 112-124, Vol. 83, No. 1
© 2002 by the Biophysical Society   0006-3495/02/07/112/13  $2.00


This article has been cited by other articles:


Home page
 Biol. Reprod.Home page
A. Uribe, T. Zarinan, M. A. Perez-Solis, R. Gutierrez-Sagal, E. Jardon-Valadez, A. Pineiro, J. A. Dias, and A. Ulloa-Aguirre
Functional and Structural Roles of Conserved Cysteine Residues in the Carboxyl-Terminal Domain of the Follicle-Stimulating Hormone Receptor in Human Embryonic Kidney 293 Cells
Biol Reprod, May 1, 2008; 78(5): 869 - 882.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
J. Zhang, C. Li, K. Chen, W. Zhu, X. Shen, and H. Jiang
Conformational transition pathway in the allosteric process of human glucokinase
PNAS, September 5, 2006; 103(36): 13368 - 13373.
[Abstract] [Full Text] [PDF]

Home page
 Protein Sci.Home page
J. Hakanpaa, G. R. Szilvay, H. Kaljunen, M. Maksimainen, M. Linder, and J. Rouvinen
Two crystal structures of Trichoderma reesei hydrophobin HFBI--The structure of a protein amphiphile with and without detergent interaction
Protein Sci., September 1, 2006; 15(9): 2129 - 2140.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
Y. Xu, J. Shen, X. Luo, W. Zhu, K. Chen, J. Ma, and H. Jiang
Conformational transition of amyloid {beta}-peptide
PNAS, April 12, 2005; 102(15): 5403 - 5407.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
X. Wang, H. P. Permentier, R. Rink, J. A. W. Kruijtzer, R. M. J. Liskamp, H. A. B. Wosten, B. Poolman, and G. T. Robillard
Probing the Self-Assembly and the Accompanying Structural Changes of Hydrophobin SC3 on a Hydrophobic Surface by Mass Spectrometry
Biophys. J., September 1, 2004; 87(3): 1919 - 1928.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. Hakanpaa, A. Paananen, S. Askolin, T. Nakari-Setala, T. Parkkinen, M. Penttila, M. B. Linder, and J. Rouvinen
Atomic Resolution Structure of the HFBII Hydrophobin, a Self-assembling Amphiphile
J. Biol. Chem., January 2, 2004; 279(1): 534 - 539.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2002 by the Biophysical Society.