Hyperstable miniproteins: additive effects of D- and L-Ala mutations

Hyperstable miniproteins: additive effects of D- and L-Ala mutations

The folding enantioselectivity for D-Ala versus L-Ala at one glycine site in the Trp-cage is 16 kJ mol(-1); judicious introductions of alanines of the correct chirality raises the melting temperature of this 20-residue fold to 83 degrees C.

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Organic & biomolecular chemistry 2008-01, Vol.6 (23), p.4287-4289
Hauptverfasser: Williams, D Victoria, Barua, Bipasha, Andersen, Niels H
Format: Artikel
Sprache:eng
Schlagworte:
Alanine - genetics
Alanine - metabolism
Amino Acid Sequence
Circular Dichroism
Magnetic Resonance Spectroscopy
Molecular Sequence Data
Mutant Proteins - chemistry
Mutant Proteins - genetics
Mutant Proteins - metabolism
Mutation
Peptides - chemistry
Peptides - genetics
Peptides - metabolism
Protein Denaturation
Stereoisomerism
Thermodynamics
Transition Temperature
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
Beschreibung
Zusammenfassung:The folding enantioselectivity for D-Ala versus L-Ala at one glycine site in the Trp-cage is 16 kJ mol(-1); judicious introductions of alanines of the correct chirality raises the melting temperature of this 20-residue fold to 83 degrees C.
ISSN:1477-0520
1477-0539
DOI:10.1039/b814314e