01810nam 2200373Ia 450 99638564100331620200824131941.0(CKB)4940000000079631(EEBO)2248541196(OCoLC)ocm12937469e(OCoLC)12937469(EXLCZ)99494000000007963119851220d1670 uy |engurbn||||a|bb|The benefit, advantage and glory of silent meetings, both as it was found at the beginning, or first breaking forth of this clear manifestation of truth, and continues so to be found, by all the faithfull and upright in heart, at this day[electronic resource] writ for the stirring up, and incouraging of these more especially who are lately convinced, unto the love of them and diligent improving them, unto those ends and uses for which they serve /given forth by George Keith ..London [s.n.]1670[2], 18, [3] pThe last three pages contain a postscript, titled, The copie of a letter written from Germany by Steven Crisp to friends ...Reproduction of original in Huntington Library.eebo-0113Society of FriendsDoctrinesSociety of FriendsDoctrines.Keith George1639?-1716.1000958Crisp Stephen1628-1692.1001337EAAEAAOCLm/cWaOLNBOOK996385641003316The benefit, advantage and glory of silent meetings, both as it was found at the beginning, or first breaking forth of this clear manifestation of truth, and continues so to be found, by all the faithfull and upright in heart, at this day2423507UNISA05897nam 2200817Ia 450 991082148060332120200520144314.0978661328285997812832828571283282852978111813703111181370359781118137048111813704397811181370171118137019(CKB)2550000000054371(EBL)818767(OCoLC)761321884(SSID)ssj0000540463(PQKBManifestationID)11324647(PQKBTitleCode)TC0000540463(PQKBWorkID)10598118(PQKB)11093674(MiAaPQ)EBC818767(Au-PeEL)EBL818767(CaPaEBR)ebr10501256(CaONFJC)MIL328285(PPN)171925513(Perlego)1011521(EXLCZ)99255000000005437120110601d2012 uy 0engur|n|---|||||txtccrProteomics of biological systems protein phosphorylation using mass spectrometry techniques /Bryan M Ham1st ed.Hoboken, N.J. John Wiley & Sons20121 online resource (376 p.)Description based upon print version of record.9781118028964 1118028961 Includes bibliographical references and index.PROTEOMICS OF BIOLOGICAL SYSTEMS: Protein Phosphorylation Using Mass Spectrometry Techniques; CONTENTS; PREFACE; ACKNOWLEDGMENTS; ABOUT THE AUTHOR; 1: Posttranslational Modification (PTM) of Proteins; 1.1 OVER 200 FORMS OF PTM OF PROTEINS; 1.2 THREE MAIN TYPES OF PTM STUDIED BY MS; 1.3 OVERVIEW OF NANO-ELECTROSPRAY/NANOFLOW LC-MS; 1.3.1 Definition and Description of MS; 1.3.2 Basic Design of Mass Analyzer Instrumentation; 1.3.3 ESI; 1.3.4 Nano-ESI; 1.4 OVERVIEW OF NUCLEIC ACIDS; 1.5 PROTEINS AND PROTEOMICS; 1.5.1 Introduction to Proteomics; 1.5.2 Protein Structure and Chemistry1.5.3 Bottom-Up Proteomics: MS of Peptides1.5.3.1 History and Strategy; 1.5.3.2 Protein Identification through Product Ion Spectra; 1.5.3.3 High-Energy Product Ions; 1.5.3.4 De Novo Sequencing; 1.5.3.5 Electron Capture Dissociation (ECD); 1.5.4 Top-Down Proteomics: MS of Intact Proteins; 1.5.4.1 Background; 1.5.4.2 GP Basicity and Protein Charging; 1.5.4.3 Calculation of Charge State and Molecular Weight; 1.5.4.4 Top-Down Protein Sequencing; 1.5.5 Systems Biology and Bioinformatics; 1.5.6 Biomarkers in Cancer; REFERENCES; 2: Glycosylation of Proteins; 2.1 PRODUCTION OF A GLYCOPROTEIN2.2 BIOLOGICAL PROCESSES OF PROTEIN GLYCOSYLATION2.3 N-LINKED AND O-LINKED GLYCOSYLATION; 2.4 CARBOHYDRATES; 2.4.1 Ionization of Oligosaccharides; 2.4.2 Carbohydrate Fragmentation; 2.4.3 Complex Oligosaccharide Structural Elucidation; 2.5 THREE OBJECTIVES IN STUDYING GLYCOPROTEINS; 2.6 GLYCOSYLATION STUDY APPROACHES; 2.6.1 MS of Glycopeptides; 2.6.2 Mass Pattern Recognition; 2.6.2.1 High Galactose Glycosylation Pattern; 2.6.3 Charge State Determination; 2.6.4 Diagnostic Fragment Ions; 2.6.5 High-Resolution/High-Mass Accuracy Measurement and Identification; 2.6.6 Digested Bovine FetuinREFERENCES3: Sulfation of Proteins as Posttranslational Modification; 3.1 GLYCOSAMINOGLYCAN SULFATION; 3.2 CELLULAR PROCESSES INVOLVED IN SULFATION; 3.3 BRIEF EXAMPLE OF PHOSPHORYLATION; 3.4 SULFOTRANSFERASE CLASS OF ENZYMES; 3.5 FRAGMENTATION NOMENCLATURE FOR CARBOHYDRATES; 3.6 SULFATED MUCIN OLIGOSACCHARIDES; 3.7 TYROSINE SULFATION; 3.8 TYROSYLPROTEIN SULFOTRANSFERASES TPST1 AND TPST2; 3.9 O-SULFATED HUMAN PROTEINS; 3.10 SULFATED PEPTIDE PRODUCT ION SPECTRA; 3.11 USE OF HIGHER ENERGY COLLISIONS; 3.12 ELECTRON CAPTURE DISSOCIATION (ECD); 3.13 SULFATION VERSUS PHOSPHORYLATION; REFERENCES4: Eukaryote PTM as Phosphorylation: Normal State Studies4.1 MASS SPECTRAL MEASUREMENT WITH EXAMPLES OF HELA CELL PHOSPHOPROTEOME; 4.1.1 Introduction; 4.1.2 Protein Phosphatase and Kinase; 4.1.3 Hydroxy-Amino Acid Phosphorylation; 4.1.4 Traditional Phosphoproteomic Approaches; 4.1.5 Current Approaches; 4.1.5.1 Phosphoproteomic Enrichment Techniques; 4.1.5.2 IMAC; 4.1.5.3 MOAC; 4.1.5.4 Methylation of Peptides prior to IMAC or MOAC Enrichment; 4.1.6 The Ideal Approach; 4.1.7 One-Dimensional (1-D) Sodium Dodecyl Sulfate (SDS) PAGE; 4.1.8 Tandem MS Approach; 4.1.8.1 pS Loss of Phosphate Group4.1.8.2 pT Loss of Phosphate GroupPhosphorylation is the addition of a phosphate (PO4) group to a protein or other organic molecule. Phosphorylation activates or deactivates many protein enzymes, causing or preventing the mechanisms of diseases such as cancer and diabetes. This book shows how to use mass spectrometry to determine whether or not a protein has been correctly modified by the addition of a phosphate group. It also provides a combination of detailed, step-by-step methodology for phosphoproteomic sample preparation, mass spectral instrumental analysis, and data interpretation approaches. Furthermore, it iProteomicsMethodologyPhosphorylationResearchMethodologyPhosphoproteinsSynthesisMass spectrometryBiological systemsResearchMethodologyProteomicsMethodology.PhosphorylationResearchMethodology.PhosphoproteinsSynthesis.Mass spectrometry.Biological systemsResearchMethodology.572/.62Ham Bryan M314951MiAaPQMiAaPQMiAaPQBOOK9910821480603321Proteomics of biological systems4092999UNINA