Amino Acid Residues at Protein−Protein Interfaces: Why Is Propensity so Different from Relative Abundance?
- 6 August 2003
- journal article
- Published by American Chemical Society (ACS) in The Journal of Physical Chemistry B
- Vol. 107 (36) , 9929-9932
- https://doi.org/10.1021/jp0348124
Abstract
No abstract availableThis publication has 10 references indexed in Scilit:
- The SWISS-PROT protein knowledgebase and its supplement TrEMBL in 2003Nucleic Acids Research, 2003
- Dynamics of Hydrogen Bond Desolvation in Protein FoldingJournal of Molecular Biology, 2002
- Prediction of protein–protein interactions by docking methodsCurrent Opinion in Structural Biology, 2002
- The 3.2-Å crystal structure of the human IgG1 Fc fragment–FcγRIII complexNature, 2000
- Convergent Solutions to Binding at a Protein-Protein InterfaceScience, 2000
- Protein structure alignment by incremental combinatorial extension (CE) of the optimal pathProtein Engineering, Design and Selection, 1998
- Inter-residue potentials in globular proteins and the dominance of highly specific hydrophilic interactions at close separation 1 1 Edited by B. HonigJournal of Molecular Biology, 1997
- Influence of water structure and of hydrophobic interactions on the strength of side‐chain hydrogen bonds in proteinsBiopolymers, 1963
- THE STRUCTURE OF WATER AND HYDROPHOBIC BONDING IN PROTEINS. III. THE THERMODYNAMIC PROPERTIES OF HYDROPHOBIC BONDS IN PROTEINS1,2The Journal of Physical Chemistry, 1962
- Thermodynamic Considerations of Protein Reactions.1,2 I. Modified Reactivity of Polar GroupsJournal of the American Chemical Society, 1954