Solution structure and interface‐driven self‐assembly of NC2, a new member of the Class II hydrophobin proteins. Issue 6 (26th December 2013)
- Record Type:
- Journal Article
- Title:
- Solution structure and interface‐driven self‐assembly of NC2, a new member of the Class II hydrophobin proteins. Issue 6 (26th December 2013)
- Main Title:
- Solution structure and interface‐driven self‐assembly of NC2, a new member of the Class II hydrophobin proteins
- Authors:
- Ren, Qin
Kwan, Ann H.
Sunde, Margaret - Abstract:
- <abstract abstract-type="main"> <title>ABSTRACT</title> <p>Hydrophobins are fungal proteins that self‐assemble spontaneously to form amphipathic monolayers at hydrophobic:hydrophilic interfaces. Hydrophobin assemblies facilitate fungal transitions between wet and dry environments and interactions with plant and animal hosts. NC2 is a previously uncharacterized hydrophobin from <italic>Neurospora crassa</italic>. It is a highly surface active protein and is able to form protein layers on a water:air interface that stabilize air bubbles. On a hydrophobic substrate, NC2 forms layers consisting of an ordered network of protein molecules, which dramatically decrease the water contact angle. The solution structure and dynamics of NC2 have been determined using nuclear magnetic resonance spectroscopy. The structure of this protein displays the same core fold as observed in other hydrophobin structures determined to date, including the Class II hydrophobins HFBI and HFBII from <italic>Trichoderma reesei</italic>, but certain features illuminate the structural differences between Classes I and II hydrophobins and also highlight the variations between structures of Class II hydrophobin family members. The unique properties of hydrophobins have attracted much attention for biotechnology applications. The insights obtained through determining the structure, biophysical properties and assembly characteristics of NC2 will facilitate the development of hydrophobin‐based applications.<abstract abstract-type="main"> <title>ABSTRACT</title> <p>Hydrophobins are fungal proteins that self‐assemble spontaneously to form amphipathic monolayers at hydrophobic:hydrophilic interfaces. Hydrophobin assemblies facilitate fungal transitions between wet and dry environments and interactions with plant and animal hosts. NC2 is a previously uncharacterized hydrophobin from <italic>Neurospora crassa</italic>. It is a highly surface active protein and is able to form protein layers on a water:air interface that stabilize air bubbles. On a hydrophobic substrate, NC2 forms layers consisting of an ordered network of protein molecules, which dramatically decrease the water contact angle. The solution structure and dynamics of NC2 have been determined using nuclear magnetic resonance spectroscopy. The structure of this protein displays the same core fold as observed in other hydrophobin structures determined to date, including the Class II hydrophobins HFBI and HFBII from <italic>Trichoderma reesei</italic>, but certain features illuminate the structural differences between Classes I and II hydrophobins and also highlight the variations between structures of Class II hydrophobin family members. The unique properties of hydrophobins have attracted much attention for biotechnology applications. The insights obtained through determining the structure, biophysical properties and assembly characteristics of NC2 will facilitate the development of hydrophobin‐based applications. Proteins 2014; 82:990–1003. © 2013 Wiley Periodicals, Inc.</p> </abstract> … (more)
- Is Part Of:
- Proteins. Volume 82:Issue 6(2014)
- Journal:
- Proteins
- Issue:
- Volume 82:Issue 6(2014)
- Issue Display:
- Volume 82, Issue 6 (2014)
- Year:
- 2014
- Volume:
- 82
- Issue:
- 6
- Issue Sort Value:
- 2014-0082-0006-0000
- Page Start:
- 990
- Page End:
- 1003
- Publication Date:
- 2013-12-26
- Subjects:
- Proteins -- Periodicals
Proteins -- Periodicals
572.6 - Journal URLs:
- http://onlinelibrary.wiley.com/ ↗
- DOI:
- 10.1002/prot.24473 ↗
- Languages:
- English
- ISSNs:
- 0887-3585
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6936.164000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 3679.xml