TY - CHAP
T1 - A computational perspective of hydrophobins through molecular dynamics simulations
AU - Patra, M.
AU - Munck, Nana
AU - Paananen, Arja
AU - Tappura, Kirsi
AU - Karttunen, M.
AU - Vattulainen, I.
PY - 2004
Y1 - 2004
N2 - Hydrophobins are small (amphiphilic) proteins specific to filamentous
fungi (~100 amino acids residues). They are among the most surface active
molecules, being responsible for the formation of hydrophobic surfaces found
in spores and fruiting bodies [1], for example. Hydrophobins are further
highly intriguing as form foaming agents, a property which has been recognized
by the beer industry. Their ability to self-assemble on the surfaces further
offers new ideas for many applications in the field of nanostructured surface
materials.
In the present work [2], we employ extensive molecular dynamics simulations to
examine structural aspects of the HFBII hydrophobin, whose crystal structure
has been determined very recently [3]. We investigate how the structure of
HFBII depends on the conditions used, including both hydrophilic and
hydrophobic environments as well as cases where the hydrophobin has placed
itself to a water-oil interface. Further, we study the self-assembly process
that is expected to be rather different from previous suggestions due to the
disulfide bridge network found in Ref. [3]. Implications of our findings are
discussed.
[1] H. A. B. Wösten and M. L. de Vocht, Biochim. Biophys. Acta 1469 (2000)
79.
[2] M. Patra, N. Munck, A. Paananen, K. Tappura, M. Karttunen, and I.
Vattulainen (to be submitted).
[3] J. Hakanpää, A. Paananen, S. Askolin, T. Nakari-Setälä, T. Parkkinen,
M. Penttilä, M. B. Linder, and J. Rouvinen, J. Biol. Chem. 279 (2004) 534.
AB - Hydrophobins are small (amphiphilic) proteins specific to filamentous
fungi (~100 amino acids residues). They are among the most surface active
molecules, being responsible for the formation of hydrophobic surfaces found
in spores and fruiting bodies [1], for example. Hydrophobins are further
highly intriguing as form foaming agents, a property which has been recognized
by the beer industry. Their ability to self-assemble on the surfaces further
offers new ideas for many applications in the field of nanostructured surface
materials.
In the present work [2], we employ extensive molecular dynamics simulations to
examine structural aspects of the HFBII hydrophobin, whose crystal structure
has been determined very recently [3]. We investigate how the structure of
HFBII depends on the conditions used, including both hydrophilic and
hydrophobic environments as well as cases where the hydrophobin has placed
itself to a water-oil interface. Further, we study the self-assembly process
that is expected to be rather different from previous suggestions due to the
disulfide bridge network found in Ref. [3]. Implications of our findings are
discussed.
[1] H. A. B. Wösten and M. L. de Vocht, Biochim. Biophys. Acta 1469 (2000)
79.
[2] M. Patra, N. Munck, A. Paananen, K. Tappura, M. Karttunen, and I.
Vattulainen (to be submitted).
[3] J. Hakanpää, A. Paananen, S. Askolin, T. Nakari-Setälä, T. Parkkinen,
M. Penttilä, M. B. Linder, and J. Rouvinen, J. Biol. Chem. 279 (2004) 534.
M3 - Conference abstract in proceedings
SN - 951-42-7129-7
T3 - Report Series in Physical Sciences
SP - 269
BT - Proceedings of the XXXVIII Annual Conference of The Finnish Physical Society. Oulu, Finland, 18 - 20 March 2004. University of Oulu. Report Series in Physical Sciences : 25
PB - University of Oulu
ER -