Sökning: WFRF:(Nielsen Line Anker) >
pH- and concentrati...
pH- and concentration-dependent supramolecular assembly of a fungal defensin plectasin variant into helical non-amyloid fibrils
-
- Pohl, Christin (författare)
- Lund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,LTH profilområde: Nanovetenskap och halvledarteknologi,LTH profilområden,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH,LTH Profile Area: Nanoscience and Semiconductor Technology,LTH Profile areas,Faculty of Engineering, LTH,Technical University of Denmark,Novozymes A/S
-
- Effantin, Gregory (författare)
- University Grenoble Alpes
-
- Kandiah, Eaazhisai (författare)
- European Synchrotron Radiation Facility
-
visa fler...
-
- Meier, Sebastian (författare)
- Technical University of Denmark
-
- Zeng, Guanghong (författare)
- Novo Nordisk A/S,Danish National Metrology Institute
-
- Streicher, Werner (författare)
- Novozymes A/S
-
- Segura, Dorotea Raventos (författare)
- Novozymes A/S
-
- Mygind, Per H. (författare)
- Novozymes A/S
-
- Sandvang, Dorthe (författare)
- Novozymes A/S
-
- Nielsen, Line Anker (författare)
- Novozymes A/S
-
- Peters, Günther H.J. (författare)
- Technical University of Denmark
-
- Schoehn, Guy (författare)
- University Grenoble Alpes
-
- Mueller-Dieckmann, Christoph (författare)
- European Synchrotron Radiation Facility
-
- Noergaard, Allan (författare)
- Novozymes A/S
-
- Harris, Pernille (författare)
- University of Copenhagen,Technical University of Denmark
-
visa färre...
-
(creator_code:org_t)
- 2022-06-07
- 2022
- Engelska.
-
Ingår i: Nature Communications. - : Springer Science and Business Media LLC. - 2041-1723. ; 13:1
- Relaterad länk:
-
http://dx.doi.org/10... (free)
-
visa fler...
-
https://lup.lub.lu.s...
-
https://doi.org/10.1...
-
visa färre...
Abstract
Ämnesord
Stäng
- Self-assembly and fibril formation play important roles in protein behaviour. Amyloid fibril formation is well-studied due to its role in neurodegenerative diseases and characterized by refolding of the protein into predominantly β-sheet form. However, much less is known about the assembly of proteins into other types of supramolecular structures. Using cryo-electron microscopy at a resolution of 1.97 Å, we show that a triple-mutant of the anti-microbial peptide plectasin, PPI42, assembles into helical non-amyloid fibrils. The in vitro anti-microbial activity was determined and shown to be enhanced compared to the wildtype. Plectasin contains a cysteine-stabilised α-helix-β-sheet structure, which remains intact upon fibril formation. Two protofilaments form a right-handed protein fibril. The fibril formation is reversible and follows sigmoidal kinetics with a pH- and concentration dependent equilibrium between soluble monomer and protein fibril. This high-resolution structure reveals that α/β proteins can natively assemble into fibrils.
Ämnesord
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Publikations- och innehållstyp
- art (ämneskategori)
- ref (ämneskategori)
Hitta via bibliotek
Till lärosätets databas
- Av författaren/redakt...
-
Pohl, Christin
-
Effantin, Gregor ...
-
Kandiah, Eaazhis ...
-
Meier, Sebastian
-
Zeng, Guanghong
-
Streicher, Werne ...
-
visa fler...
-
Segura, Dorotea ...
-
Mygind, Per H.
-
Sandvang, Dorthe
-
Nielsen, Line An ...
-
Peters, Günther ...
-
Schoehn, Guy
-
Mueller-Dieckman ...
-
Noergaard, Allan
-
Harris, Pernille
-
visa färre...
- Om ämnet
-
- NATURVETENSKAP
-
NATURVETENSKAP
-
och Biologi
-
och Biokemi och mole ...
- Artiklar i publikationen
-
Nature Communica ...
- Av lärosätet
-
Lunds universitet