LEADER 01442nam--2200457---450- 001 990001304580203316 005 20061108132036.0 010 $a2-07-021319-6 035 $a000130458 035 $aUSA01000130458 035 $a(ALEPH)000130458USA01 035 $a000130458 100 $a20031217d2005----km-y0itaa50------ba 101 0 $afre 102 $aFR 105 $ay|||z|||001yy 200 1 $aÉtudes de style$fLéo Spitzer$gprécédé de Léo Spitzer et la lecture stylistique par Jean Starobinski$gtraduit de l'anglais et de l'allemand par Éliane Kaufholz, Alain Coulon, Michel Foucault 210 $aParis$cGallimard$dstampa 2005 215 $a531 p.$d19 cm 225 2 $aTel$v54 410 0$12001$aTel$v54 517 $aLéo Spitzer et la lecture stylistique 606 0 $aStilistica 606 0 $aLetteratura francese 676 $a808 700 1$aSPITZER,$bLeo$0132452 702 1$aSTAROBINSKI,$bJean 702 1$aKAUFHOLZ,$bÉliane 702 1$aCOULON,$bAlain 702 1$aFOUCAULT,$bMichel 801 0$aIT$bsalbc$gISBD 912 $a990001304580203316 951 $aVIII.3. 84$b189286 L.M.$cVIII.3.$d00125004 959 $aBK 969 $aUMA 979 $aMARIA$b10$c20031217$lUSA01$h1048 979 $aPATRY$b90$c20040406$lUSA01$h1732 979 $aJOHNNY$b90$c20040414$lUSA01$h1220 979 $aANNAMARIA$b90$c20061108$lUSA01$h1320 996 $aEtudes de style$9193460 997 $aUNISA LEADER 05088nam 2200661Ia 450 001 9910830708903321 005 20210811191859.0 010 $a1-283-37152-9 010 $a9786613371522 010 $a0-470-60260-0 010 $a0-470-60261-9 035 $a(CKB)2480000000008330 035 $a(EBL)698738 035 $a(OCoLC)815646392 035 $a(SSID)ssj0000550585 035 $a(PQKBManifestationID)11337038 035 $a(PQKBTitleCode)TC0000550585 035 $a(PQKBWorkID)10509441 035 $a(PQKB)11323714 035 $a(MiAaPQ)EBC698738 035 $a(PPN)194589781 035 $a(EXLCZ)992480000000008330 100 $a20090527d2010 uy 0 101 0 $aeng 135 $aur|n|---||||| 181 $ctxt 182 $cc 183 $acr 200 00$aInstrumental analysis of intrinsically disordered proteins $eassessing structure and conformation /$fedited by Vladimir N. Uversky and Sonia Longhi 210 $aHoboken, N.J. $cWiley$dc2010 215 $a1 online resource (792 p.) 225 1 $aWiley series on protein and peptide science 300 $aDescription based upon print version of record. 311 $a0-470-34341-9 320 $aIncludes bibliographical references and index. 327 $aINSTRUMENTAL ANALYSIS OF INTRINSICALLY DISORDERED PROTEINS: Assessing Structure and Conformation; CONTENTS; PREFACE; INTRODUCTION TO THE WILEY SERIES ON PROTEIN AND PEPTIDE SCIENCE; LIST OF CONTRIBUTORS; LIST OF ABBREVIATIONS; PART I: ASSESSING IDPs IN THE LIVING CELL; 1: IDPs AND PROTEIN DEGRADATION IN THE CELL; 2: THE STRUCTURAL BIOLOGY OF IDPs INSIDE CELLS; PART II: SPECTROSCOPIC TECHNIQUES; 3: NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY APPLIED TO (INTRINSICALLY) DISORDERED PROTEINS; 4: ATOMIC-LEVEL CHARACTERIZATION OF DISORDERED PROTEIN ENSEMBLES USING NMR RESIDUAL DIPOLAR COUPLINGS 327 $a5: DETERMINING STRUCTURAL ENSEMBLES FOR INTRINSICALLY DISORDERED PROTEINS6: SITE-DIRECTED SPIN LABELING EPR SPECTROSCOPY; 7: THE STRUCTURE OF UNFOLDED PEPTIDES AND PROTEINS EXPLORED BY VIBRATIONAL SPECTROSCOPY; 8: INTRINSICALLY DISORDERED PROTEINS AND INDUCED FOLDING STUDIED BY FOURIER TRANSFORM INFRARED SPECTROSCOPY; 9: GENETICALLY ENGINEERED POLYPEPTIDES AS A MODEL OF INTRINSICALLY DISORDERED FIBRILLOGENIC PROTEINS: DEEP UV RESONANCE RAMAN SPECTROSCOPIC STUDY; 10: CIRCULAR DICHROISM OF INTRINSICALLY DISORDERED PROTEINS; 11: FLUORESCENCE SPECTROSCOPY OF INTRINSICALLY DISORDERED PROTEINS 327 $a12: HYDRATION OF INTRINSICALLY DISORDERED PROTEINS FROM WIDE-LINE NMRPART III: SINGLE-MOLECULE TECHNIQUES; 13: SINGLE-MOLECULE SPECTROSCOPY OF UNFOLDED PROTEINS; 14: MONITORING THE CONFORMATIONAL EQUILIBRIA OF MONOMERIC INTRINSICALLY DISORDERED PROTEINS BY SINGLE-MOLECULE FORCE SPECTROSCOPY; PART IV: METHODS TO ASSESS PROTEIN SIZE AND SHAPE; 15: ANALYTICAL ULTRACENTRIFUGATION, A USEFUL TOOL TO PROBE INTRINSICALLY DISORDERED PROTEINS; 16: STRUCTURAL INSIGHTS INTO INTRINSICALLY DISORDERED PROTEINS BY SMALL-ANGLE X-RAY SCATTERING; 17: DYNAMIC AND STATIC LIGHT SCATTERING 327 $a18: ANALYZING INTRINSICALLY DISORDERED PROTEINS BY SIZE EXCLUSION CHROMATOGRAPHYPART V: CONFORMATIONAL STABILITY; 19: CONFORMATIONAL BEHAVIOR OF INTRINSICALLY DISORDERED PROTEINS: EFFECTS OF STRONG DENATURANTS, TEMPERATURE, PH , COUNTERIONS, AND MACROMOLECULAR CROWDING; 20: DETECTING DISORDERED REGIONS IN PROTEINS BY LIMITED PROTEOLYSIS; PART VI: MASS SPECTROMETRY; 21: MASS SPECTROMETRY TOOLS FOR THE INVESTIGATION OF STRUCTURAL DISORDER AND CONFORMATIONAL TRANSITIONS IN PROTEINS; PART VII: EXPRESSION AND PURIFICATION OF IDPS 327 $a22: RECOMBINANT PRODUCTION OF INTRINSICALLY DISORDERED PROTEINS FOR BIOPHYSICAL AND STRUCTURAL CHARACTERIZATION23: LARGE-SCALE IDENTIFICATION OF INTRINSICALLY DISORDERED PROTEINS; 24: PURIFICATION OF INTRINSICALLY DISORDERED PROTEINS; INDEX; Colour plates 330 $aInstrumental techniques for analyzing intrinsically disordered proteins The recently recognized phenomenon of protein intrinsic disorder is gaining significant interest among researchers, especially as the number of proteins and protein domains that have been shown to be intrinsically disordered rapidly grows. The first reference to tackle this little-documented area, Instrumental Analysis of Intrinsically Disordered Proteins: Assessing Structure and Conformation provides researchers with a much-needed, comprehensive summary of recent achievements in the methods for structural 410 0$aWiley series in protein and peptide science. 606 $aProteins$xAnalysis 606 $aProteins$xConformation 606 $aProteins$xDenaturation 615 0$aProteins$xAnalysis. 615 0$aProteins$xConformation. 615 0$aProteins$xDenaturation. 676 $a572.633 701 $aLonghi$b Sonia$01602216 701 $aUversky$b Vladimir N$0873541 801 0$bMiAaPQ 801 1$bMiAaPQ 801 2$bMiAaPQ 906 $aBOOK 912 $a9910830708903321 996 $aInstrumental analysis of intrinsically disordered proteins$93932650 997 $aUNINA