LEADER 03285nam 2200601Ia 450 001 9910877567303321 005 20200520144314.0 010 $a1-280-36766-0 010 $a9786610367665 010 $a0-470-34930-1 010 $a0-471-46523-2 010 $a0-471-22442-1 035 $a(CKB)111056485567976 035 $a(EBL)152017 035 $a(SSID)ssj0000330178 035 $a(PQKBManifestationID)11247018 035 $a(PQKBTitleCode)TC0000330178 035 $a(PQKBWorkID)10318593 035 $a(PQKB)10617485 035 $a(MiAaPQ)EBC152017 035 $a(OCoLC)53796107 035 $a(EXLCZ)99111056485567976 100 $a20011119d2002 uy 0 101 0 $aeng 135 $aur|n|---||||| 181 $ctxt 182 $cc 183 $acr 200 00$aComputational methods for protein folding /$fedited by Richard A. Friesner 210 $aNew York $cWiley$d2002 215 $a1 online resource (546 p.) 225 1 $aAdvances in chemical physics ;$vv. 120 300 $aDescription based upon print version of record. 311 $a0-471-20955-4 327 $aCOMPUTATIONAL METHODS FOR PROTEIN FOLDING A SPECIAL VOLUME OF ADVANCES IN CHEMICAL PHYSICS VOLUME 120; CONTRIBUTORS TO VOLUME 120; INTRODUCTION; PREFACE; CONTENTS; STATISTICAL ANALYSIS OF PROTEIN FOLDING KINETICS; INSIGHTS INTO SPECIFIC PROBLEMS IN PROTEIN FOLDING USING SIMPLE CONCEPTS; PROTEIN RECOGNITION BY SEQUENCE-TO-STRUCTURE FITNESS: BRIDGING EFFICIENCY AND CAPACITY OF THREADING MODELS; A UNIFIED APPROACH TO THE PREDICTION OF PROTEIN STRUCTURE AND FUNCTION; KNOWLEDGE-BASED PREDICTION OF PROTEIN TERTIARY STRUCTURE 327 $aAB INITIO PROTEIN STRUCTURE PREDICTION USING A SIZE-DEPENDENT TERTIARY FOLDING POTENTIALDETERMINISTIC GLOBAL OPTIMIZATION AND AB INITIO APPROACHES FOR THE STRUCTURE PREDICTION OF POLYPEPTIDES, DYNAMICS OF PROTEIN FOLDING, AND PROTEIN-PROTEIN INTERACTIONS; DETECTING NATIVE PROTEIN FOLDS AMONG LARGE DECOY SITES WITH THE OPLS ALL-ATOM POTENTIAL AND THE SURFACE GENERALIZED BORN SOLVENT MODEL; AUTHOR INDEX; SUBJECT INDEX 330 $aSince the first attempts to model proteins on a computer began almost thirty years ago, our understanding of protein structure and dynamics has dramatically increased. Spectroscopic measurement techniques continue to improve in resolution and sensitivity, allowing a wealth of information to be obtained with regard to the kinetics of protein folding and unfolding, and complementing the detailed structural picture of the folded state. Concurrently, algorithms, software, and computational hardware have progressed to the point where both structural and kinetic problems may be studied with a fair d 410 0$aAdvances in chemical physics ;$vv. 120. 606 $aProtein folding$xMathematical models 606 $aProteins$xConformation$xMathematical models 615 0$aProtein folding$xMathematical models. 615 0$aProteins$xConformation$xMathematical models. 676 $a541.305 676 $a541/.08 676 $a547.75 701 $aFriesner$b Richard A$01753755 801 0$bMiAaPQ 801 1$bMiAaPQ 801 2$bMiAaPQ 906 $aBOOK 912 $a9910877567303321 996 $aComputational methods for protein folding$94189756 997 $aUNINA