Автор: Jenner Matthew Название: Using Mass Spectrometry for Biochemical Studies on Enzymatic Domains from Polyketide Synthases ISBN: 3319813552 ISBN-13(EAN): 9783319813554 Издательство: Springer Рейтинг: Цена: 93160.00 T Наличие на складе: Есть у поставщика Поставка под заказ. Описание: This thesis reports studies on the substrate specificity of crucial ketosynthase (KS) domains from trans-AT Polyketide Synthases (PKSs). Using a combination of electrospray ionisation-mass spectrometry (ESI-MS) and simple N-acetyl cysteamine (SNAC) substrate mimics, the specificity of a range of KS domains from the bacillaene and psymberin PKSs have been succsessfully studied with regard to the initial acylation step of KS-catalysis. In addition, the ability to alter the substrate tolerance of KS domains by simple point mutations in the active site has been demonstrated. A series of acyl-ACPs have been synthesised using a novel methodology and employed to probe the substrate specificity of both KS domains and the previously uncharcterised acyl hydrolase domain, PedC. KS-catalysed chain elongation reactions have also been conducted and monitored by ESI-MS/MS. All KS domains studied exhibited higher substrate specificity at the elongation step than in the preceeding acylation step. Furthermore, a mechanism of reversible acylation is proposed using the PsyA ACP1-KS1 di-domain. The findings in this thesis provide important insights into mechanisms of KS specificity and show that mutagenesis can be used to expand the repertoire of acceptable substrates for future PKS engineering.
Автор: Kazuya Machida; Bernard A. Liu Название: SH2 Domains ISBN: 1493967606 ISBN-13(EAN): 9781493967605 Издательство: Springer Рейтинг: Цена: 167700.00 T Наличие на складе: Есть у поставщика Поставка под заказ. Описание:
Preface... Table of Contents... Contributing Authors...
Part I Overview
1. Introduction: History of SH2 Domains and Their Applications Bernard A. Liu and Kazuya Machida 2. What Have We Learned from SH2 Domains? Bruce J. Mayer Part II Computational Approaches 3. Hidden Markov Models for Protein Domain Homology Identification and Analysis Karl Jablonowski 4. Classification and Lineage Tracing of SH2 Domains Throughout Eukaryotes Bernard A. Liu 5. SH2 Ligand Prediction-Guidance for In-Silico Screening Shawn S.C. Li and Lei Li 6. An Efficient Semi-Supervised Learning Approach to Predict SH2 Domain Mediated Interactions Kousik Kundu and Rolf Backofen 7. Proteomic Clustering Analysis of SH2 Domain DatasetsKarl Jablonowski Part III Experimental Tools 8. Expression and Production of SH2 Domain Proteins Bernard A. Liu, Mari Ogiue-Ikeda, and Kazuya Machida 9. Expression and Purification of Soluble STAT5b/STAT3 Proteins for SH2 Domain Binding Assay Akira Asai and Kazuyuki Takakuma 10. Purification of SOCS (Suppressors of Cytokine Signalling) SH2 Domains for Structural and Functional Studies Nicholas P.D. Liau, Artem Laktyushin, and Jeffrey J. Babon 11. Expression and Purification of SH2 Domains Using Baculovirus Expression System Mari Ogiue-Ikeda and Kazuya Machida 12. Functionally Altered SH2 Domains for Biochemical Studies: Loss of Function Mutant and Domain Concatenation Mari Ogiue-Ikeda and Kazuya Machida 13. Creation of Phosphotyrosine Superbinders by Directed Evolution of an SH2 Domain Haiming Huang, Tomonori Kaneko, Sachdev S. Sidhu, and Shawn S.C. Li Part IV Structural Analysis and Binding Assays 14. Structural Characterization of Monomeric/Dimeric State of p59fyn SH2 Domain Radu Huculeci, Fabien Kieken, Abel Garcia-Pino, Lieven Buts, Nico van Nuland, and Tom Lenaerts 15. NMR Chemical Shift Mapping of SH2 Peptide Interactions Marissa A. McKercher and Deborah S. Wuttke 16. Calorimetric Measurement of SH2 Domain Ligand Affinities Marissa A. McKercher and Deborah S. Wuttke 17. Binding Assays Using Recombinant SH2 Domains: Far-Western, Pull Down, and Fluorescence Polarization Kazuya Machida and Bernard A. Liu 18. In-Solution SH2 Domain Binding Assay Based on Proximity Ligation Kazuya Machida Part V High-Throughput Screening and Proteomics 19. Alpha-Based Multiplexed Assay for Identifying SH2 Domain Antagonists Akira Asai and Kazuyuki Takakuma 20. Characterizing SH2 Domain Specificity and Network Interactions Using SPOT Peptide Arrays Bernard A. Liu 21. High Throughput Quantification of SH2 Domain-Phosphopeptide Interactions with Cellulose Peptide Conjugate Microarrays Brett W. Engelmann 22. SH2 Domains as Affinity Reagents for Phosphotyrosine Protein Enrichment and Proteomic Analysis Mi Ke, Bizhu Chu, Lin Lin, and Ruijun Tian 23. Identification of Tyrosine Phosphorylated Proteins by SH2 Domain Affinity Purification and Mass Spectrometry Sophia Buhs, Helwe Gerull, and Peter Nollau 24. Analysis of the Global Changes in SH2 Binding Properties Using Mass Spectrometry Supported by Quantitative Stable Isotope Labeling by Amino Acids in Cell Culture (SILAC) Technique Radoslaw M. Sobota 25. Using Reciprocal Protein-Peptide Array Screening to Unravel Protein Interaction Networks Huadong Liu, Courtney Voss, and Shawn Shun-Ch
Автор: Matthew Jenner Название: Using Mass Spectrometry for Biochemical Studies on Enzymatic Domains from Polyketide Synthases ISBN: 3319327224 ISBN-13(EAN): 9783319327228 Издательство: Springer Рейтинг: Цена: 95770.00 T Наличие на складе: Есть у поставщика Поставка под заказ. Описание: Introduction.- Materials and Methods.- Substrate Specificity of Ketosynthase Domains Part I: β-Branched Acyl Chains.- Substrate Specificity of Ketosynthase Domains Part II: Amino Acid-Containing Acyl Chains.- Synthesis of Acyl-Acyl Carrier Proteins and their use in Studying Polyketide Synthase Enzymology.- Substrate Specificity of Ketosynthase Domains Part III: Elongation-Based Substrate Specificity.
Автор: Natalya Kurochkina Название: SH Domains ISBN: 3319372521 ISBN-13(EAN): 9783319372525 Издательство: Springer Рейтинг: Цена: 111790.00 T Наличие на складе: Есть у поставщика Поставка под заказ. Описание: This book covers structure, function, and important roles of the SH domains, structure-function relationships, the versatile nature of their action, mechanisms of aggregation, specificity of interactions, impact of mutations on protein functional dysregulation, and cell signaling. Their involvement in various cellular processes such as migration, invasiveness, actin reorganization, shaping spines, determination of the morphology assembly of fibrils, and mechanotransduction makes these molecules attractive drug targets. Substrates, inhibitors and activators of PTKs present a wide variety of therapeutic agents in the context of delivering treatments for numerous pathologies. The new emerging field of stem cell therapies and design of biomaterials for treatments relies on the directed regulation of stem cell growth, differentiation and morphology, as well as the production of biomimetic scaffolds that respond to programmed signals. Advances in deciphering the mechanisms of action of these important molecules will lead to the implementation and success of their vital applications.
Автор: Kenworthy,Anne Название: Lipid Domains,75 ISBN: 0128032952 ISBN-13(EAN): 9780128032954 Издательство: Elsevier Science Рейтинг: Цена: 159450.00 T Наличие на складе: Есть у поставщика Поставка под заказ.
Автор: Natalya Kurochkina Название: SH Domains ISBN: 3319200976 ISBN-13(EAN): 9783319200972 Издательство: Springer Рейтинг: Цена: 121110.00 T Наличие на складе: Есть у поставщика Поставка под заказ. Описание: This book covers structure, function, and important roles of the SH domains, structure-function relationships, the versatile nature of their action, mechanisms of aggregation, specificity of interactions, impact of mutations on protein functional dysregulation, and cell signaling.
Автор: Ludwig Heilmeyer Название: Interacting Protein Domains ISBN: 3642645836 ISBN-13(EAN): 9783642645839 Издательство: Springer Рейтинг: Цена: 121110.00 T Наличие на складе: Есть у поставщика Поставка под заказ. Описание: Proceedings of the NATO Advanced Study Institute on Structure and Function of Interacting Protein Domains in Signal and Energy Transduction, held at Acquafredda di Maratea, Italy, September 10-19, 1996
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