Hydrophobin Film Structure for HFBI and HFBII and Mechanism for Accelerated Film Formation

Aniket Magarkar, Nawel Mele, Noha Abdel-Rahman, Sarah Butcher, Mika Torkkeli, Ritva Serimaa, Arja Paananen, Markus Linder, Alex Bunker (Corresponding Author)

Research output: Contribution to journalArticleScientificpeer-review

16 Citations (Scopus)

Abstract

Hydrophobins represent an important group of proteins from both a biological and nanotechnological standpoint. They are the means through which filamentous fungi affect their environment to promote growth, and their properties at interfaces have resulted in numerous applications. In our study we have combined protein docking, molecular dynamics simulation, and electron cryo-microscopy to gain atomistic level insight into the surface structure of films composed of two class II hydrophobins: HFBI and HFBII produced by Trichoderma reesei. Together our results suggest a unit cell composed of six proteins; however, our computational results suggest P6 symmetry, while our experimental results show P3 symmetry with a unit cell size of 56 Å. Our computational results indicate the possibility of an alternate ordering with a three protein unit cell with P3 symmetry and a smaller unit cell size, and we have used a Monte Carlo simulation of a spin model representing the hydrophobin film to show how this alternate metastable structure may play a role in increasing the rate of surface coverage by hydrophobin films, possibly indicating a mechanism of more general significance to both biology and nanotechnology.
Original languageEnglish
Article numbere1003745
JournalPLoS Computational Biology
Volume10
Issue number7
DOIs
Publication statusPublished - 2014
MoE publication typeA1 Journal article-refereed

Fingerprint

films (materials)
Proteins
Protein
symmetry
Unit
protein
Cell Size
Symmetry
Alternate
Computational Results
proteins
cells
Cryoelectron Microscopy
Trichoderma reesei
nanotechnology
Trichoderma
Nanotechnology
molecular dynamics
Docking
Cell

Cite this

Magarkar, A., Mele, N., Abdel-Rahman, N., Butcher, S., Torkkeli, M., Serimaa, R., ... Bunker, A. (2014). Hydrophobin Film Structure for HFBI and HFBII and Mechanism for Accelerated Film Formation. PLoS Computational Biology, 10(7), [e1003745]. https://doi.org/10.1371/journal.pcbi.1003745
Magarkar, Aniket ; Mele, Nawel ; Abdel-Rahman, Noha ; Butcher, Sarah ; Torkkeli, Mika ; Serimaa, Ritva ; Paananen, Arja ; Linder, Markus ; Bunker, Alex. / Hydrophobin Film Structure for HFBI and HFBII and Mechanism for Accelerated Film Formation. In: PLoS Computational Biology. 2014 ; Vol. 10, No. 7.
@article{b18f6d6729554da88a7e9234994b8756,
title = "Hydrophobin Film Structure for HFBI and HFBII and Mechanism for Accelerated Film Formation",
abstract = "Hydrophobins represent an important group of proteins from both a biological and nanotechnological standpoint. They are the means through which filamentous fungi affect their environment to promote growth, and their properties at interfaces have resulted in numerous applications. In our study we have combined protein docking, molecular dynamics simulation, and electron cryo-microscopy to gain atomistic level insight into the surface structure of films composed of two class II hydrophobins: HFBI and HFBII produced by Trichoderma reesei. Together our results suggest a unit cell composed of six proteins; however, our computational results suggest P6 symmetry, while our experimental results show P3 symmetry with a unit cell size of 56 {\AA}. Our computational results indicate the possibility of an alternate ordering with a three protein unit cell with P3 symmetry and a smaller unit cell size, and we have used a Monte Carlo simulation of a spin model representing the hydrophobin film to show how this alternate metastable structure may play a role in increasing the rate of surface coverage by hydrophobin films, possibly indicating a mechanism of more general significance to both biology and nanotechnology.",
author = "Aniket Magarkar and Nawel Mele and Noha Abdel-Rahman and Sarah Butcher and Mika Torkkeli and Ritva Serimaa and Arja Paananen and Markus Linder and Alex Bunker",
year = "2014",
doi = "10.1371/journal.pcbi.1003745",
language = "English",
volume = "10",
journal = "PLoS Computational Biology",
issn = "1553-734X",
publisher = "Public Library of Science",
number = "7",

}

Magarkar, A, Mele, N, Abdel-Rahman, N, Butcher, S, Torkkeli, M, Serimaa, R, Paananen, A, Linder, M & Bunker, A 2014, 'Hydrophobin Film Structure for HFBI and HFBII and Mechanism for Accelerated Film Formation', PLoS Computational Biology, vol. 10, no. 7, e1003745. https://doi.org/10.1371/journal.pcbi.1003745

Hydrophobin Film Structure for HFBI and HFBII and Mechanism for Accelerated Film Formation. / Magarkar, Aniket; Mele, Nawel; Abdel-Rahman, Noha; Butcher, Sarah; Torkkeli, Mika; Serimaa, Ritva; Paananen, Arja; Linder, Markus; Bunker, Alex (Corresponding Author).

In: PLoS Computational Biology, Vol. 10, No. 7, e1003745, 2014.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Hydrophobin Film Structure for HFBI and HFBII and Mechanism for Accelerated Film Formation

AU - Magarkar, Aniket

AU - Mele, Nawel

AU - Abdel-Rahman, Noha

AU - Butcher, Sarah

AU - Torkkeli, Mika

AU - Serimaa, Ritva

AU - Paananen, Arja

AU - Linder, Markus

AU - Bunker, Alex

PY - 2014

Y1 - 2014

N2 - Hydrophobins represent an important group of proteins from both a biological and nanotechnological standpoint. They are the means through which filamentous fungi affect their environment to promote growth, and their properties at interfaces have resulted in numerous applications. In our study we have combined protein docking, molecular dynamics simulation, and electron cryo-microscopy to gain atomistic level insight into the surface structure of films composed of two class II hydrophobins: HFBI and HFBII produced by Trichoderma reesei. Together our results suggest a unit cell composed of six proteins; however, our computational results suggest P6 symmetry, while our experimental results show P3 symmetry with a unit cell size of 56 Å. Our computational results indicate the possibility of an alternate ordering with a three protein unit cell with P3 symmetry and a smaller unit cell size, and we have used a Monte Carlo simulation of a spin model representing the hydrophobin film to show how this alternate metastable structure may play a role in increasing the rate of surface coverage by hydrophobin films, possibly indicating a mechanism of more general significance to both biology and nanotechnology.

AB - Hydrophobins represent an important group of proteins from both a biological and nanotechnological standpoint. They are the means through which filamentous fungi affect their environment to promote growth, and their properties at interfaces have resulted in numerous applications. In our study we have combined protein docking, molecular dynamics simulation, and electron cryo-microscopy to gain atomistic level insight into the surface structure of films composed of two class II hydrophobins: HFBI and HFBII produced by Trichoderma reesei. Together our results suggest a unit cell composed of six proteins; however, our computational results suggest P6 symmetry, while our experimental results show P3 symmetry with a unit cell size of 56 Å. Our computational results indicate the possibility of an alternate ordering with a three protein unit cell with P3 symmetry and a smaller unit cell size, and we have used a Monte Carlo simulation of a spin model representing the hydrophobin film to show how this alternate metastable structure may play a role in increasing the rate of surface coverage by hydrophobin films, possibly indicating a mechanism of more general significance to both biology and nanotechnology.

U2 - 10.1371/journal.pcbi.1003745

DO - 10.1371/journal.pcbi.1003745

M3 - Article

VL - 10

JO - PLoS Computational Biology

JF - PLoS Computational Biology

SN - 1553-734X

IS - 7

M1 - e1003745

ER -