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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 |
|---|---|
| Otros Autores: | |
| Formato: | Electrónico eBook |
| Idioma: | Inglés |
| Publicado: |
Berlin :
De Gruyter,
2011.
|
| Temas: | |
| Acceso en línea: | Texto completo |
MARC
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| 049 | |a UAMI | ||
| 245 | 0 | 0 | |a Methods in protein biochemistry / |c edited by Harald Tschesche. |
| 260 | |a Berlin : |b De Gruyter, |c 2011. | ||
| 300 | |a 1 online resource (xxvi, 378 pages) : |b color illustrations, portrait | ||
| 336 | |a text |b txt |2 rdacontent | ||
| 337 | |a computer |b c |2 rdamedia | ||
| 338 | |a online resource |b cr |2 rdacarrier | ||
| 347 | |a text file |b PDF |2 rda | ||
| 504 | |a Includes bibliographical references and index. | ||
| 505 | 0 | |a 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. | |
| 505 | 8 | |a 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. | |
| 505 | 8 | |a 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. | |
| 505 | 8 | |a 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. | |
| 505 | 8 | |a 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. | |
| 500 | |a 9.3 Cofactors in biology provide spectroscopic access to reaction cycles. | ||
| 520 | |a 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. | ||
| 588 | 0 | |a Print version record. | |
| 546 | |a In English. | ||
| 590 | |a ProQuest Ebook Central |b Ebook Central Academic Complete | ||
| 590 | |a eBooks on EBSCOhost |b EBSCO eBook Subscription Academic Collection - Worldwide | ||
| 650 | 0 | |a Proteins |x Analysis. | |
| 650 | 0 | |a Proteins |x Chemical warfare. | |
| 650 | 0 | |a Proteomics |x Methods. | |
| 650 | 2 | 2 | |a Proteomics |x methods |
| 650 | 1 | 2 | |a Proteins |x chemistry |
| 650 | 1 | 2 | |a Proteins |x analysis |
| 650 | 2 | 2 | |a Proteins |x isolation & purification |
| 650 | 4 | |a Analytische Methoden. | |
| 650 | 4 | |a Biochemie. | |
| 650 | 4 | |a Proteine. | |
| 650 | 6 | |a Protéines |x Analyse. | |
| 650 | 6 | |a Protéines |x Guerre chimique. | |
| 650 | 7 | |a SCIENCE |x Life Sciences |x Biochemistry. |2 bisacsh | |
| 650 | 7 | |a Proteins |x Analysis |2 fast | |
| 650 | 7 | |a Proteomics |2 fast | |
| 655 | 7 | |a Methods (Music) |2 fast | |
| 700 | 1 | |a Tschesche, Harald. | |
| 758 | |i has work: |a Methods in protein biochemistry (Text) |1 https://id.oclc.org/worldcat/entity/E39PCGfFbffqmBMM6YQGTrwMrm |4 https://id.oclc.org/worldcat/ontology/hasWork | ||
| 776 | 0 | 8 | |i Print version: |a Tschesche, Harald. |t Methods in Protein Biochemistry. |d Berlin : De Gruyter, ©2011 |z 9783110252330 |
| 856 | 4 | 0 | |u https://ebookcentral.uam.elogim.com/lib/uam-ebooks/detail.action?docID=835445 |z Texto completo |
| 880 | 0 | 0 | |6 505-00/(S |t Frontmatter -- |t Preface -- |t Editor. List of contributing authors -- |t Contents -- |t Abbreviations -- |t Acknowledgements -- |t 1 Three-phase partitioning -- |t 2 Folding and degradation functions of molecular chaperones -- |t 3 Membrane protein folding in detergents -- |t 4 Glycoprotein-folding quality control in the endoplasmic reticulum -- |t 5 Conformational dynamics in peptides and proteins studied by triplet-triplet energy transfer -- |t 6 Protein import into the intermembrane space of mitochondria -- |t 7 On-membrane identification of gel-resolved proteins by matrix-assisted laser desorption ionization mass spectrometry (MALDI-MS) -- |t 8 Analysis of protein complexes using chemical cross-linking and mass spectrometry -- |t 9 Single-crystal spectroscopy correlated with X-ray crystallography provides complementary perspectives on macromolecular function -- |t 10 Wide-angle X-ray solution scattering (WAXS) -- |t 11 Where purity matters: recombinant versus synthetic peptides in beta amyloid formation -- |t 12 Chemical modifi cation of proteins in living cells -- |t 13 Proteomics of human bronchoalveolar lavage fluid: discovery of biomarkers of chronic obstructive pulmonary disease (COPD) with difference gel electrophoresis (DIGE) and mass spectrometry (MS) -- |t 14 Proteomic analysis of Duchenne muscular dystrophy (DMD) -- |t 15 Target-oriented peptide arrays in a palliative approach to cystic fibrosis (CF) -- |t 16 Probing protein dynamics in vivo using backbone cyclization: bacterial acyl carrier protein as a case study -- |t 17 The protein epitope mimetic approach to protein-protein interaction inhibitors -- |t 18 The structural biology of α1-antitrypsin deficiency and the serpinopathies -- |t Index. |
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