1;Preface;62;Editor;83;Contents;124;List of contributing authors;85;Abbreviations;186;Acknowledgements;267;1 Three-phase partitioning;287.1;1.1 Method;297.2;1.2 The mechanism of TPP;307.3;1.3 A practical example - the isolation of cathepsin L from liver tissue;317.4;1.4 Other applications;328;2 Folding and degradation functions of molecular chaperones;408.1;2.1 Introduction;408.2;2.2 The domain structure of Hsc/Hsp70;408.3;2.3 The Hsc/Hsp70 reaction cycle;428.4;2.4 Cochaperones determine the function of Hsc/Hsp70;438.5;2.5 In vitro reconstitution and functional analysis of the Hsc/Hsp70 chaperone system;438.6;2.6 Measuring the ATPase activity of Hsc/Hsp70;458.7;2.7 Determining chaperone activity;458.8;2.8 In vitro reconstitution of chaperone-assisted ubiquitylation;468.9;2.9 Concluding remarks;489;3 Membrane protein folding in detergents;509.1;3.1 Introduction;509.2;3.2 Interactions of membrane proteins with detergents;519.3;3.3 Techniques to characterize TM proteins in detergents;569.4;3.4 Applications of TM protein-detergent complexes;629.5;3.5 Conclusions;6810;4 Glycoprotein-folding quality control in the endoplasmic reticulum;7410.1;4.1 Introduction;7410.2;4.2 Glycoprotein-folding quality control (QC);7410.3;4.3 The UGGT;7610.4;4.4 GII;7910.5;4.5 CNX and CRT;8110.6;4.6 ERp57;8410.7;4.7 Methods to study glycoprotein folding QC;8511;5 Conformational dynamics in peptides and proteins studied by triplet-triplet energy transfer;10011.1;5.1 Introduction;10011.2;5.2 Concept of TTET experiments to study intrachain loop formation in polypeptide chains;10011.3;5.3 Diffusion-controlled loop formation in unstructured polypeptide chains;10611.4;5.4 Detection of fast conformational fluctuations in folded peptides and proteins by TTET;11211.5;5.5 Conclusions;11812;6 Protein import into the intermembrane space of mitochondria;12212.1;6.1 Introduction;12212.2;6.2 The mitochondrial IMS;12212.3;6.3 The mitochondrial disulfide relay;12312.4;6.4 The sulfhydryl oxidase Erv1;12312.5;6.5 The oxidoreductase Mia40;12512.6;6.6 Substrates of the mitochondrial disulfide relay;12512.7;6.7 Methods to study mitochondrial protein translocation;12612.8;6.8 General comments to the analysis of thiol-disulfide redox states;13212.9;6.9 Outlook;13413;7 On-membrane identification of gel-resolved proteins by matrix-assisted laser desorption ionization mass spectrometry (MALDI-MS);14013.1;7.1 Introduction;14013.2;7.2 Methods for identifying proteins electroblotted onto the PVDF membrane;14313.3;7.3 General comments to the analysis of proteins on membranes;14513.4;7.4 PVDF membranes or diamond-like carbon-coated (DLC) stainless steel plates?;15113.5;7.5 Concluding remarks;15114;8 Analysis of protein complexes using chemical cross-linking and mass spectrometry;15414.1;8.1 Introduction;15414.2;8.2 Reagents for chemical cross-linking;15414.3;8.3 The chemical cross-linking workflow;15814.4;8.4 MS and data analysis;16014.5;8.5 Practical examples;16314.6;8.6 The use of spatial constraints for modeling;16414.7;8.7 Conclusion and outlook;16515;9 Single-crystal spectroscopy correlated with X-ray crystallography provides complementary perspectives on macromolecular function;17015.1;9.1 Introduction;17015.2;9.2 Ionizing radiation: essential for crystal structures; a problem and a reagent17315.3;9.3 Cofactors in biology provide spectroscopic access to reaction cycles;17415.4;9.4 Single-crystal spectroscopy correlated with X-ray diffraction;17715.5;9.5 Correlated studies at beamline X26-C of the NSLS;18015.6;9.6 Future prospects;18616;10 Wide-angle X-ray solution scattering (WAXS);19216.1;10.1 Introduction;19216.2;10.2 Sample preparation;19316.3;10.3 Sample-handling robot;19416.4;10.4 Data collection;19516.5;10.5 Data processing;19616.6;10.6 Structural information;19816.7;10.7 Size and shape;19816.8;10.8 Secondary and tertiary structure;19916.9;10.9 Quaternary structure;20016.10;10.10 Structural c