Calmodulin interacts with amphiphilic peptides composed of all D-amino acids

CALMODULIN binds to amphiphilic, helical peptides of a variety of amino-acid sequences 1–8 . These peptides are usually positively charged, although there is spectroscopic evidence that at least one neutral peptide binds 5 . The complex between calmodulin and one of its natural target peptides, the...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	Nature (London) 1994-04, Vol.368 (6472), p.651-653
Hauptverfasser:	Fisher, Phyllis J., Prendergast, Franklyn G., Ehrhardt, Mark R., Urbauer, Jeffrey L., Wand, A. Joshua, Sedarous, Salah S., McCormick, Daniel J., Buckley, Paul J.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino acids Analytical, structural and metabolic biochemistry Binding and carrier proteins Binding Sites Biochemistry Biological and medical sciences Calmodulin - metabolism Calmodulin-Binding Proteins - metabolism Circular Dichroism Crystallography Fluorescence Polarization Fundamental and applied biological sciences. Psychology Humanities and Social Sciences letter Melitten - metabolism multidisciplinary Myosin-Light-Chain Kinase - metabolism Peptides Peptides - metabolism Protein Binding Proteins Science Science (multidisciplinary) Spectrophotometry, Ultraviolet Stereoisomerism
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Schreiben Sie den ersten Kommentar!