Geometric analysis of cross-linkability for protein fold discrimination.
Protein structure provides insight into the evolutionary origins, functions, and mechanisms of proteins. We are pursuing a minimalist approach to protein fold identification that characterizes possible folds in terms of consistency of their geometric features with restraints derived from relatively cheap, high-throughput experiments. One such experiment is residue-specific cross-linking analyzed by mass spectrometry. This paper presents a suite of novel lower- and upper-bounding algorithms for analyzing the distance between surface cross-link sites and thereby validating predicted models against experimental cross-linking results. Through analysis and computational experiments, using simulated and published experimental data, we demonstrate that our algorithms enable effective model discrimination.
Dept of Comp. Sci., Purdue Univ., West Lafayette, IN 47907, USA.
S
S
Potluri
A A
AA
Khan
A
A
Kuzminykh
J M
JM
Bujnicki
A M
AM
Friedman
C
C
Bailey-Kellogg
D000465:Algorithms; D001665:Binding Sites; D019295:Computational Biology; D003198:Computer Simulation; D003432:Cross-Linking Reagents; D013058:Mass Spectrometry; D008958:Models, Molecular; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry
D003432:Cross-Linking Reagents; D011506:Proteins