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Methods in protein biochemistry
Title statement Methods in protein biochemistry [elektronický zdroj] / edited by Harald Tschesche Issue data Berlin : De Gruyter, 2011 Phys.des. 1 online zdroj (xxvi, 378 s.) : il., portréty ISBN 9783110252361 (e-book) 3110252368 (e-book) Note 9.3 Cofactors in biology provide spectroscopic access to reaction cycles. Popsáno podle tištěné verze Internal Bibliographies/Indexes Note Obsahuje bibliografické odkazy a rejstřík Contents Preface; Editor; List of contributing authors; Abbreviations; Acknowledgements; 1 Three-phase partitioning; 1.1 Method; 1.2 The mechanism of TPP; 1.3 A practical example -- the isolation of cathepsin L from liver tissue; 1.4 Other applications; 2 Folding and degradation functions of molecular chaperones; 2.1 Introduction; 2.2 The domain structure of Hsc/Hsp70; 2.3 The Hsc/Hsp70 reaction cycle; 2.4 Cochaperones determine the function of Hsc/Hsp70; 2.5 In vitro reconstitution and functional analysis of the Hsc/Hsp70 chaperone system; 2.6 Measuring the ATPase activity of Hsc/Hsp70. Content note 2.7 Determining chaperone activity2.8 In vitro reconstitution of chaperone-assisted ubiquitylation; 2.9 Concluding remarks; 3 Membrane protein folding in detergents; 3.1 Introduction; 3.2 Interactions of membrane proteins with detergents; 3.3 Techniques to characterize TM proteins in detergents; 3.4 Applications of TM protein-detergent complexes; 3.5 Conclusions; 4 Glycoprotein-folding quality control in the endoplasmic reticulum; 4.1 Introduction; 4.2 Glycoprotein-folding quality control (QC); 4.3 The UGGT; 4.4 GII; 4.5 CNX and CRT; 4.6 ERp57; 4.7 Methods to study glycoprotein folding QC.. 5 Conformational dynamics in peptides and proteins studied by triplet-triplet energy transfer5.1 Introduction; 5.2 Concept of TTET experiments to study intrachain loop formation in polypeptide chains; 5.3 Diffusion-controlled loop formation in unstructured polypeptide chains; 5.4 Detection of fast conformational fluctuations in folded peptides and proteins by TTET; 5.5 Conclusions; 6 Protein import into the intermembrane space of mitochondria; 6.1 Introduction; 6.2 The mitochondrial IMS; 6.3 The mitochondrial disulfide relay; 6.4 The sulfhydryl oxidase Erv1; 6.5 The oxidoreductase Mia40.. 6.6 Substrates of the mitochondrial disulfide relay6.7 Methods to study mitochondrial protein translocation; 6.8 General comments to the analysis of thiol-disulfide redox states; 6.9 Outlook; 7 On-membrane identification of gel-resolved proteins by matrix-assisted laser desorption ionization mass spectrometry (MALDI-MS); 7.1 Introduction; 7.2 Methods for identifying proteins electroblotted onto the PVDF membrane; 7.3 General comments to the analysis of proteins on membranes; 7.4 PVDF membranes or diamond-like carbon-coated (DLC) stainless steel plates?; 7.5 Concluding remarks.. 8 Analysis of protein complexes using chemical cross-linking and mass spectrometry8.1 Introduction; 8.2 Reagents for chemical cross-linking; 8.3 The chemical cross-linking workflow; 8.4 MS and data analysis; 8.5 Practical examples; 8.6 The use of spatial constraints for modeling; 8.7 Conclusion and outlook; 9 Single-crystal spectroscopy correlated with X-ray crystallography provides complementary perspectives on macromolecular function; 9.1 Introduction; 9.2 Ionizing radiation: essential for crystal structures; a problem and a reagent. Notes to Availability Přístup pouze pro oprávněné uživatele Note Způsob přístupu: World Wide Web Another responsib. Tschesche, Harald (editor) Subj. Headings biochemie biochemistry * bílkoviny proteins * proteomika proteomics * chemické zbraně chemical weapons Form, Genre elektronické knihy electronic books Conspect 577 - Biochemie. Molekulární biologie. Biofyzika UDC 577.1 , 577.112 , 623.459 , 577.112.01:575.111 , (0.034.2:08) Country Německo Language angličtina Document kind Electronic sources URL http://search.ebscohost.com/login.aspx?direct=true&scope=site&db=nlebk&db=nlabk&AN=430064 
book
This book presents a survey of recent developments in protein biochemistry. Top researchers in the field of protein biochemistry describe modern methods to address the challenges of protein purification by three-phase partitioning, and their folding and degradation by the functions of chaperones. The significance of peptide purity for fibril formation is addressed as well as the use of target oriented peptide arrays in palliative approaches in mucoviszidose. The design and application of protein epitope mimetics just as the structural resolving of the misfolding of various mutant proteins in s.
Preface; Editor; List of contributing authors; Abbreviations; Acknowledgements; 1 Three-phase partitioning; 1.1 Method; 1.2 The mechanism of TPP; 1.3 A practical example -- the isolation of cathepsin L from liver tissue; 1.4 Other applications; 2 Folding and degradation functions of molecular chaperones; 2.1 Introduction; 2.2 The domain structure of Hsc/Hsp70; 2.3 The Hsc/Hsp70 reaction cycle; 2.4 Cochaperones determine the function of Hsc/Hsp70; 2.5 In vitro reconstitution and functional analysis of the Hsc/Hsp70 chaperone system; 2.6 Measuring the ATPase activity of Hsc/Hsp70.2.7 Determining chaperone activity2.8 In vitro reconstitution of chaperone-assisted ubiquitylation; 2.9 Concluding remarks; 3 Membrane protein folding in detergents; 3.1 Introduction; 3.2 Interactions of membrane proteins with detergents; 3.3 Techniques to characterize TM proteins in detergents; 3.4 Applications of TM protein-detergent complexes; 3.5 Conclusions; 4 Glycoprotein-folding quality control in the endoplasmic reticulum; 4.1 Introduction; 4.2 Glycoprotein-folding quality control (QC); 4.3 The UGGT; 4.4 GII; 4.5 CNX and CRT; 4.6 ERp57; 4.7 Methods to study glycoprotein folding QC.5 Conformational dynamics in peptides and proteins studied by triplet-triplet energy transfer5.1 Introduction; 5.2 Concept of TTET experiments to study intrachain loop formation in polypeptide chains; 5.3 Diffusion-controlled loop formation in unstructured polypeptide chains; 5.4 Detection of fast conformational fluctuations in folded peptides and proteins by TTET; 5.5 Conclusions; 6 Protein import into the intermembrane space of mitochondria; 6.1 Introduction; 6.2 The mitochondrial IMS; 6.3 The mitochondrial disulfide relay; 6.4 The sulfhydryl oxidase Erv1; 6.5 The oxidoreductase Mia40.6.6 Substrates of the mitochondrial disulfide relay6.7 Methods to study mitochondrial protein translocation; 6.8 General comments to the analysis of thiol-disulfide redox states; 6.9 Outlook; 7 On-membrane identification of gel-resolved proteins by matrix-assisted laser desorption ionization mass spectrometry (MALDI-MS); 7.1 Introduction; 7.2 Methods for identifying proteins electroblotted onto the PVDF membrane; 7.3 General comments to the analysis of proteins on membranes; 7.4 PVDF membranes or diamond-like carbon-coated (DLC) stainless steel plates?; 7.5 Concluding remarks.8 Analysis of protein complexes using chemical cross-linking and mass spectrometry8.1 Introduction; 8.2 Reagents for chemical cross-linking; 8.3 The chemical cross-linking workflow; 8.4 MS and data analysis; 8.5 Practical examples; 8.6 The use of spatial constraints for modeling; 8.7 Conclusion and outlook; 9 Single-crystal spectroscopy correlated with X-ray crystallography provides complementary perspectives on macromolecular function; 9.1 Introduction; 9.2 Ionizing radiation: essential for crystal structures; a problem and a reagent.
Number of the records: 1