A computational perspective of hydrophobins through molecular dynamics simulations

M. Patra, Nana Munck, Arja Paananen, Kirsi Tappura, M. Karttunen, I. Vattulainen

Research output: Chapter in Book/Report/Conference proceedingConference abstract in proceedingsScientific

Abstract

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.
Original languageEnglish
Title of host publicationProceedings 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
PublisherUniversity of Oulu
Pages269
Number of pages1
ISBN (Electronic)951-42-7287-0
ISBN (Print)951-42-7129-7
Publication statusPublished - 2004

Publication series

NameReport Series in Physical Sciences
PublisherUniversity of Oulu
Number25
ISSN (Print)1239-4327

Fingerprint

Molecular dynamics
Computer simulation
Beer
Blowing agents
Fungi
Disulfides
Self assembly
Oils
Crystal structure
Amino Acids
Molecules
Water
Industry
Proteins

Cite this

Patra, M., Munck, N., Paananen, A., Tappura, K., Karttunen, M., & Vattulainen, I. (2004). A computational perspective of hydrophobins through molecular dynamics simulations. In 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 (pp. 269). University of Oulu. Report Series in Physical Sciences, No. 25
Patra, M. ; Munck, Nana ; Paananen, Arja ; Tappura, Kirsi ; Karttunen, M. ; Vattulainen, I. / A computational perspective of hydrophobins through molecular dynamics simulations. 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. University of Oulu, 2004. pp. 269 (Report Series in Physical Sciences; No. 25).
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Patra, M, Munck, N, Paananen, A, Tappura, K, Karttunen, M & Vattulainen, I 2004, A computational perspective of hydrophobins through molecular dynamics simulations. in 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. University of Oulu, Report Series in Physical Sciences, no. 25, pp. 269.

A computational perspective of hydrophobins through molecular dynamics simulations. / Patra, M.; Munck, Nana; Paananen, Arja; Tappura, Kirsi; Karttunen, M.; Vattulainen, I.

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. University of Oulu, 2004. p. 269 (Report Series in Physical Sciences; No. 25).

Research output: Chapter in Book/Report/Conference proceedingConference abstract in proceedingsScientific

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 -

Patra M, Munck N, Paananen A, Tappura K, Karttunen M, Vattulainen I. A computational perspective of hydrophobins through molecular dynamics simulations. In 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. University of Oulu. 2004. p. 269. (Report Series in Physical Sciences; No. 25).