Accurate computer-based design of a new backbone conformation in the second turn of protein L
- 18 January 2002
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 315 (3) , 471-477
- https://doi.org/10.1006/jmbi.2001.5229
Abstract
No abstract availableKeywords
This publication has 22 references indexed in Scilit:
- Manipulation of ligand binding affinity by exploitation of conformational coupling.Nature Structural & Molecular Biology, 2001
- Computer-based redesign of a protein folding pathway.Nature Structural & Molecular Biology, 2001
- Structures of the B1 domain of protein L fromPeptostreptococcus magnuswith a tyrosine to tryptophan substitutionActa Crystallographica Section D-Biological Crystallography, 2001
- Computational design of an integrin I domain stabilized in the open high affinity conformation.Nature Structural & Molecular Biology, 2000
- A breakdown of symmetry in the folding transition state of protein LJournal of Molecular Biology, 2000
- Side-chain and backbone flexibility in protein core designJournal of Molecular Biology, 1999
- High-Resolution Protein Design with Backbone FreedomScience, 1998
- De Novo Protein Design: Fully Automated Sequence SelectionScience, 1997
- Coupling backbone flexibility and amino acid sequence selection in protein designProtein Science, 1997
- De novo design of the hydrophobic cores of proteinsProtein Science, 1995