SOLUTION STRUCTURE OF AN HGR INHIBITOR, NMR, 10 STRUCTURES
Denaturation and reactivation of dimeric human glutathione reductase--an assay for folding inhibitors.
SIMULATED-ANNEALING PROTOCOL STARTING WITH 50 RANDOM STRUCTURES. 236 DISTANCE CONSTRAINTS. ENERGY MINIMIZED (2000 CYCLES), SUBJECTED TO ROOM-TEMPERATURE-RESTRAINED MOLECULAR DYNAMICS (20PS) AND ENERGY MINIMIZED AGAIN (2000 CYCLES). AFTER THIS, NO DISTANCE OR DIHEDRAL-ANGLE CONSTRAINTS WERE VIOLATED. FINAL REFINEMENT: ENERGY MINIMIZATION ON THE BASIS OF THE COMPLETE EMPIRICAL-ENERGY FUNCTION (DEFAULT PARAMETERS BUT DIELECTRIC CONSTANT E OF 3) INCLUDING THE ELECTROSTATIC INTERACTIONS.
HUMAN GLUTATHIONE REDUCTASE, PROTEIN-DIMERIZATION INHIBITOR, OXIDOREDUCTASE
ACRQEPQPQGPPPAAGAVASYDYLVIGGGSGGLASARRAAELGARAAVVESHKLGGTCVNVGCVPKKVMWNTAVHSEFMH DHADYGFPSCEGKFNWRVIKEKRDAYVSRLNAIYQNNLTKSHIEIIRGHAAFTSDPKPTIEVSGKKYTAPHILIATGGMP STPHESQIPGASLGITSDGFFQLEELPGRSVIVGAGYIAVEMAGILSALGSKTSLMIRHDKVLRSFDSMISTNCTEELEN AGVEVLKFSQVKEVKKTLSGLEVSMVTAVPGRLPVMTMIPDVDCLLWAIGRVPNTKDLSLNKLGIQTDDKGHIIVDEFQN TNVKGIYAVGDVCGKALLTPVAIAAGRKLAHRLFEYKEDSKLDYNNIPTVVFSHPPIGTVGLTEDEAIHKYGIENVKTYS TSFTPMYHAVTKRKTKCVMKMVCANKEEKVVGIHMQGLGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSEELVTLR