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Methods in protein biochemistry /
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. Th...
| Clasificación: | Libro Electrónico |
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| Otros Autores: | |
| Formato: | Electrónico eBook |
| Idioma: | Inglés |
| Publicado: |
Berlin :
De Gruyter,
2011.
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| Temas: | |
| Acceso en línea: | Texto completo |
Tabla de Contenidos:
- 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.