Additivity-based prediction of equilibrium constants for some protein-protein associations.
For many protein families, such as serine proteinases or serine proteinase inhibitors, the family assignment predicts reactivity only in general terms. Both detailed specificity and quantitative reactivity are lacking. We believe that, for many such protein families, algorithms can be devised by defining the subset of n functionally important sequence positions, making the 19n possible single mutants and measuring their reactivity. Given the assumption that the contributions of the n positions are additive, the reactivities of the 20(n) variants can be predicted. This is illustrated by an almost complete algorithm for the Kazal family of protein inhibitors of serine proteinases.
Laskowski
Michael
M
Department of Chemistry, Purdue University, 560 Oval Drive, West Lafayette, IN 47907-2084, USA. michael.laskowski.1@purdue.edu
Qasim
M A
MA
Yi
ZhengPing
Z
D000465:Algorithms; D001665:Binding Sites; D004735:Energy Transfer; D046911:Macromolecular Substances; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry* / Q000145:classification* / Q000235:genetics; D016415:Sequence Alignment / Q000379:methods*; D020539:Sequence Analysis, Protein / Q000379:methods*; D014359:Trypsin Inhibitor, Kazal Pancreatic / Q000737:chemistry / Q000145:classification
D046911:Macromolecular Substances; D011506:Proteins; D014359:Trypsin Inhibitor, Kazal Pancreatic