PolyQ aggregation studied by model peptides with intrinsic tryptophan fluorophores
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource
- Language
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Englisch
- Bibliographic citation
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In: Biophysical Chemistry ; 284 (2022). - 106782. - Elsevier. - ISSN 0301-4622. - eISSN 1873-4200
- Event
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Veröffentlichung
- (where)
-
Konstanz
- (who)
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KOPS Universität Konstanz
- (when)
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2022
- Creator
- URN
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urn:nbn:de:bsz:352-2-1ivwon2i4ulyh7
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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25.03.2025, 1:43 PM CET
Data provider
This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Siu, Ho-Wah
- Stritt, Paul
- Zhao, Heng
- Hauser, Karin
- KOPS Universität Konstanz
Time of origin
- 2022
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Synthesis and analysis of model peptides containing oxidized tryptophan residues
Modulation of amyloid peptides aggregation by hydrophilic polymers
Atomistic Simulations of Amyloidogenic Peptides and Their Aggregation
PolyQ aggregation studied by ATR-FTIR difference spectroscopy
Metal-induced aggregation of ß-peptides on membrane surfaces
Identifizierung von Tryptophanderivaten in Tryptophan, tryptophanhaltigen Peptiden und Proteinen : = Identification of contaminants in biotechnologically manufactured tryptophan and oxidation of tryptophan residues in peptides and proteins
Self-assembly of transmembrane peptides studied by solid-state NMR
Interaction and aggregation mechanisms of peptides at biologically relevant interfaces
Aggregation of Transmembrane Peptides Studied by Spin-Label EPR
Spontaneous aggregation of fibril-forming peptides studied by Molecular Dynamics simulations
Arginine and Tryptophan rich antimicrobial peptides (AMP)
Folding and aggregation of amyloid peptides
Synthesis and analysis of model peptides containing oxidized tryptophan residues
Modulation of amyloid peptides aggregation by hydrophilic polymers
Atomistic Simulations of Amyloidogenic Peptides and Their Aggregation
PolyQ aggregation studied by ATR-FTIR difference spectroscopy
Metal-induced aggregation of ß-peptides on membrane surfaces
Identifizierung von Tryptophanderivaten in Tryptophan, tryptophanhaltigen Peptiden und Proteinen : = Identification of contaminants in biotechnologically manufactured tryptophan and oxidation of tryptophan residues in peptides and proteins
Self-assembly of transmembrane peptides studied by solid-state NMR
Interaction and aggregation mechanisms of peptides at biologically relevant interfaces
Aggregation of Transmembrane Peptides Studied by Spin-Label EPR
Spontaneous aggregation of fibril-forming peptides studied by Molecular Dynamics simulations
Arginine and Tryptophan rich antimicrobial peptides (AMP)
Folding and aggregation of amyloid peptides
Synthesis and analysis of model peptides containing oxidized tryptophan residues
Modulation of amyloid peptides aggregation by hydrophilic polymers
Atomistic Simulations of Amyloidogenic Peptides and Their Aggregation
PolyQ aggregation studied by ATR-FTIR difference spectroscopy
Metal-induced aggregation of ß-peptides on membrane surfaces
Identifizierung von Tryptophanderivaten in Tryptophan, tryptophanhaltigen Peptiden und Proteinen : = Identification of contaminants in biotechnologically manufactured tryptophan and oxidation of tryptophan residues in peptides and proteins
Self-assembly of transmembrane peptides studied by solid-state NMR