A Dominant Conformational Role for Amino Acid Diversity in Minimalist Protein–Protein Interfaces
- 12 June 2008
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 381 (2) , 407-418
- https://doi.org/10.1016/j.jmb.2008.06.014
Abstract
No abstract availableKeywords
This publication has 30 references indexed in Scilit:
- The Intrinsic Contributions of Tyrosine, Serine, Glycine and Arginine to the Affinity and Specificity of AntibodiesJournal of Molecular Biology, 2008
- Exploring the Capacity of Minimalist Protein Interfaces: Interface Energetics and Affinity Maturation to Picomolar KD of a Single-domain Antibody with a Flat ParatopeJournal of Molecular Biology, 2007
- High-affinity single-domain binding proteins with a binary-code interfaceProceedings of the National Academy of Sciences, 2007
- Coot: model-building tools for molecular graphicsActa Crystallographica Section D-Biological Crystallography, 2004
- WebLogo: A Sequence Logo Generator: Figure 1Genome Research, 2004
- Refinement of Macromolecular Structures by the Maximum-Likelihood MethodActa Crystallographica Section D-Biological Crystallography, 1997
- [20] Processing of X-ray diffraction data collected in oscillation modePublished by Elsevier ,1997
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994
- Shape Complementarity at Protein/Protein InterfacesJournal of Molecular Biology, 1993
- Sequence logos: a new way to display consensus sequencesNucleic Acids Research, 1990