Side Chain Orientation of Tryptophan Analogues Determines Agonism and Inverse Agonism in Short Ghrelin Peptides
- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
Online-Ressource
- Language
-
Englisch
- Bibliographic citation
-
Side Chain Orientation of Tryptophan Analogues Determines Agonism and Inverse Agonism in Short Ghrelin Peptides ; volume:14 ; number:21 ; year:2019 ; pages:1849-1855 ; extent:7
ChemMedChem ; 14, Heft 21 (2019), 1849-1855 (gesamt 7)
- Creator
-
Nicke, Lennart
Müller, Ronny
Geyer, Armin
Els‐Heindl, Sylvia
- DOI
-
10.1002/cmdc.201900409
- URN
-
urn:nbn:de:101:1-2022081005455658031092
- Rights
-
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
15.08.2025, 7:34 AM CEST
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
- Nicke, Lennart
- Müller, Ronny
- Geyer, Armin
- Els‐Heindl, Sylvia
Other Objects (12)
Studies on tryptophan analogues in proteins
Studies on tryptophan analogues in proteins
Synthesis of constrained analogues of tryptophan
Incorporation of tryptophan analogues into the lantibiotic nisin
Arginine and Tryptophan rich antimicrobial peptides (AMP)
Iron‐Catalyzed Biomimetic Dimerization of Tryptophan‐Containing Peptides
Iron‐Catalyzed Biomimetic Dimerization of Tryptophan‐Containing Peptides
Synthesis and analysis of model peptides containing oxidized tryptophan residues
Gold-catalyzed direct alkynylation of tryptophan in peptides using TIPS-EBX
PolyQ aggregation studied by model peptides with intrinsic tryptophan fluorophores
Hierarchical assembly of tryptophan zipper peptides into stress-relaxing bioactive hydrogels
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
Studies on tryptophan analogues in proteins
Studies on tryptophan analogues in proteins
Synthesis of constrained analogues of tryptophan
Incorporation of tryptophan analogues into the lantibiotic nisin
Arginine and Tryptophan rich antimicrobial peptides (AMP)
Iron‐Catalyzed Biomimetic Dimerization of Tryptophan‐Containing Peptides
Iron‐Catalyzed Biomimetic Dimerization of Tryptophan‐Containing Peptides
Synthesis and analysis of model peptides containing oxidized tryptophan residues
Gold-catalyzed direct alkynylation of tryptophan in peptides using TIPS-EBX
PolyQ aggregation studied by model peptides with intrinsic tryptophan fluorophores
Hierarchical assembly of tryptophan zipper peptides into stress-relaxing bioactive hydrogels
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
Studies on tryptophan analogues in proteins
Studies on tryptophan analogues in proteins
Synthesis of constrained analogues of tryptophan
Incorporation of tryptophan analogues into the lantibiotic nisin
Arginine and Tryptophan rich antimicrobial peptides (AMP)
Iron‐Catalyzed Biomimetic Dimerization of Tryptophan‐Containing Peptides
Iron‐Catalyzed Biomimetic Dimerization of Tryptophan‐Containing Peptides
Synthesis and analysis of model peptides containing oxidized tryptophan residues
Gold-catalyzed direct alkynylation of tryptophan in peptides using TIPS-EBX
PolyQ aggregation studied by model peptides with intrinsic tryptophan fluorophores
Hierarchical assembly of tryptophan zipper peptides into stress-relaxing bioactive hydrogels