LEADER 00970nam0 2200277 i 450 001 VAN0001343 005 20111012025345.918 100 $a20020701d1994 |0itac50 ba 101 $aita 102 $aIT 105 $a|||| ||||| 200 1 $aManuale di diritto commerciale$fAlessandro Graziani 205 $a2. ed 210 $aNapoli$cA. Morano$d1994 215 $a767 p.$d22 cm. 606 $aDiritto commerciale$3VANC000927$2FI 620 $dNapoli$3VANL000005 676 $a347.7$v21 700 1$aGraziani$bAlessandro$f1900-1962$3VANV001311$0132933 712 $aMorano$3VANV108283$4650 801 $aIT$bSOL$c20230616$gRICA 899 $aBIBLIOTECA DEL DIPARTIMENTO DI GIURISPRUDENZA$1IT-CE0105$2VAN00 912 $aVAN0001343 950 $aBIBLIOTECA DEL DIPARTIMENTO DI GIURISPRUDENZA$d00CONS VI.C.8 $e00 4951 20020910 996 $aManuale di diritto commerciale$941116 997 $aUNICAMPANIA LEADER 05480nam 2200697 a 450 001 9910825812403321 005 20240313151638.0 010 $a1-299-24119-0 010 $a3-527-63185-2 010 $a3-527-63184-4 035 $a(CKB)3280000000000413 035 $a(EBL)1129766 035 $a(OCoLC)829460537 035 $a(SSID)ssj0000622245 035 $a(PQKBManifestationID)11407601 035 $a(PQKBTitleCode)TC0000622245 035 $a(PQKBWorkID)10655009 035 $a(PQKB)10519290 035 $a(OCoLC)847669975 035 $a(MiAaPQ)EBC1129766 035 $a(Au-PeEL)EBL1129766 035 $a(CaPaEBR)ebr10662565 035 $a(CaONFJC)MIL455369 035 $a(EXLCZ)993280000000000413 100 $a20130307d2012 uy 0 101 0 $aeng 135 $aurcn||||||||| 181 $ctxt 182 $cc 183 $acr 200 00$aAnalysis and function of amino acids and peptides /$fedited by Andrew B. Hughes 205 $a1st ed. 210 $aWeinheim, Germany $cWiley-VCH$d2012 215 $a1 online resource (510 p.) 225 0 $aAmino acids, peptides and proteins in organic chemistry ;$vv. 5 300 $aDescription based upon print version of record. 311 $a3-527-32104-7 320 $aIncludes bibliographical references and index. 327 $aAmino Acids, Peptides and Proteins in Organic Chemistry:Volume 5 - Analysis and Function of Amino Acids and Peptides; Contents; List of Contributors; 1 Mass Spectrometry of Amino Acids and Proteins; 1.1 Introduction; 1.1.1 Mass Terminology; 1.1.2 Components of a Mass Spectrometer; 1.1.3 Resolution and Mass Accuracy; 1.1.4 Accurate Analysis of ESI Multiply Charged Ions; 1.1.5 Fragment Ions; 1.2 Basic Protein Chemistry and How it Relates to MS; 1.2.1 Mass Properties of the Polypeptide Chain; 1.2.2 In Vivo Protein Modifications; 1.2.3 Ex Vivo Protein Modifications 327 $a1.3 Sample Preparation and Data Acquisition 1.3.1 Top-Down Versus Bottom-Up Proteomics; 1.3.2 Shotgun Versus Targeted Proteomics; 1.3.3 Enzymatic Digestion for Bottom-Up Proteomics; 1.3.4 Liquid Chromatography and Capillary Electrophoresis for Mixtures in Bottom-Up; 1.4 Data Analysis of LC-MS/MS (or CE-MS/MS) of Mixtures; 1.4.1 Identification of Proteins from MS/MS Spectra of Peptides; 1.4.2 De Novo Sequencing; 1.5 MS of Protein Structure, Folding, and Interactions; 1.5.1 Methods to Mass-Tag Structural Features; 1.6 Conclusions and Perspectives; References 327 $a2 X-Ray Structure Determination of Proteins and Peptides 2.1 Introduction; 2.1.1 Light Microscopy; 2.1.2 X-Rays and Crystallography at the Start; 2.1.3 X-Ray Crystallography Today; 2.1.4 Limitations of X-Ray Crystallography; 2.2 Growing Crystals; 2.2.1 Why Crystals?; 2.2.2 Basic Methods of Growing Protein Crystals; 2.2.3 Protein Sample; 2.2.4 Preliminary Crystal Analysis; 2.2.5 Mounting Crystals for X-Ray Analysis; 2.3 Symmetry and Space Groups; 2.3.1 Crystals and the Unit Cell; 2.3.2 Point Groups; 2.3.3 Space Groups; 2.3.4 Asymmetric Unit; 2.4 X-Ray Scattering and Diffraction 327 $a2.4.1 X-Rays and Mathematical Representation of Waves 2.4.2 Interaction of X-Rays with Matter; 2.4.3 Crystal Lattice, Miller Indices, and the Reciprocal Space; 2.4.4 X-Ray Diffraction from a Crystal: Bragg.s Law; 2.4.5 Bragg.s Law in Reciprocal Space; 2.4.6 Fourier Transform Equation from a Lattice; 2.4.7 Friedel' s Law and the Electron Density Equation; 2.5 Collecting and Processing Diffraction Data; 2.5.1 Data Collection Strategy; 2.5.2 Symmetry and Scaling Data; 2.6 Solving the Structure (Determining Phases); 2.6.1 Molecular Replacement; 2.6.2 Isomorphous Replacement; 2.6.3 MAD 327 $a2.7 Analyzing and Refining the Structure 2.7.1 Electron Density Interpretation and Model Building; 2.7.2 Protein Structure Refinement; 2.7.3 Protein Structure Validation; References; 3 Nuclear Magnetic Resonance of Amino Acids, Peptides, and Proteins; 3.1 Introduction; 3.1.1 Active Nuclei in NMR; 3.1.2 Energy Levels and Spin States; 3.1.3 Main NMR Parameters (Glossary); 3.1.3.1 Chemical Shift; 3.1.3.2 Scalar Coupling Constants; 3.1.3.3 NOE; 3.1.3.4 RDC; 3.2 Amino Acids; 3.2.1 Historical Significance; 3.2.2 Amino Acids Structure; 3.2.3 Random Coil Chemical Shift; 3.2.4 Spin Systems 327 $a3.2.5 Labile Protons 330 $aThis is the last of five books in the Amino Acids, Peptides and Proteins in Organic Synthesis series. Closing a gap in the literature, this is the only series to cover this important topic in organic and biochemistry. Drawing upon the combined expertise of the international ""who's who"" in amino acid research, these volumes represent a real benchmark for amino acid chemistry, providing a comprehensive discussion of the occurrence, uses and applications of amino acids and, by extension, their polymeric forms, peptides and proteins. The practical value of each volume is 410 0$aAmino Acids, Peptides and Proteins in Organic Chemistry (VCH) 606 $aAmino acids$xAnalysis 606 $aPeptides$xAnalysis 606 $aProteins$xAnalysis 615 0$aAmino acids$xAnalysis. 615 0$aPeptides$xAnalysis. 615 0$aProteins$xAnalysis. 676 $a547.7 701 $aHughes$b Andrew B$0521472 801 0$bMiAaPQ 801 1$bMiAaPQ 801 2$bMiAaPQ 906 $aBOOK 912 $a9910825812403321 996 $aAnalysis and function of amino acids and peptides$94104953 997 $aUNINA