Keywords:
Medicine.
;
Electronic books.
Type of Medium:
Online Resource
Pages:
1 online resource (276 pages)
Edition:
1st ed.
ISBN:
9784431558408
URL:
https://ebookcentral.proquest.com/lib/geomar/detail.action?docID=4403295
DDC:
572.8
Language:
English
Note:
Intro -- Foreword -- Preface -- Contents -- Chapter 1: Time-Resolved Detection of Protein Fluctuations During Reactions -- 1.1 Introduction -- 1.1.1 Fluctuations of Biomolecules -- 1.1.2 Time-Resolved Detection of Fluctuations -- 1.2 Methods -- 1.2.1 The Transient Grating (TG) Method -- 1.2.2 The Transient Lens (TrL) Method -- 1.2.3 Thermodynamical Properties -- 1.3 Fluctuations During Reactions -- 1.3.1 Ligand Dissociation of Carbonmonoxymyoglobin (MbCO) -- 1.3.2 Fluctuation During the Photoreaction of PYP -- 1.3.3 Fluctuation During the Photoreaction of the Phototropin LOV Domain -- 1.3.3.1 LOV2 Domain -- 1.3.3.2 Reaction of the LOV2-Linker -- 1.4 Summary -- References -- Chapter 2: Pressure Perturbation: A Prime Tool to Study Conformational Substates and Volume Fluctuations of Biomolecular Assem... -- 2.1 Introduction -- 2.2 Elucidation of Conformational Substates and Volume Fluctuations in Biomolecules Using Pressure Perturbation Approaches -- 2.2.1 Determination of Fluctuation Parameters -- 2.3 Conformational Fluctuations, Substates, and Phase Transitions of Biomolecular Systems Revealed by Pressure Perturbation -- 2.3.1 Lipid Membranes -- 2.3.1.1 Effects of Pressure on the Structure, Phase Behavior, and Dynamics of Lipid Membranes -- 2.3.2 Proteins in Bulk Solution -- 2.3.3 Protein Aggregation and Amyloid Formation -- 2.3.4 Membrane-Associated Biomolecular Assemblies -- 2.4 Outlook -- References -- Chapter 3: Watching a Signaling Protein Function in Real Time via Picosecond Time-Resolved Laue Crystallography -- 3.1 Introduction -- 3.2 Experimental Methodology -- 3.2.1 Crystal Preparation -- 3.2.2 Pump-Probe Method -- 3.2.2.1 Laser Source (Pump) -- 3.2.2.2 X-Ray Source (Probe) -- 3.2.2.3 Pump-Probe Time Delay -- 3.2.2.4 Data Collection Protocol -- 3.2.3 Data Reduction and Analysis Methodologies -- 3.2.3.1 Interpolated Ratio Method.
,
3.2.3.2 Excitation Degree Scaling -- 3.2.3.3 Rhkl Merging -- 3.2.3.4 Time-Dependent Electron Density Map Generation -- 3.2.3.5 Real-Space Global Analysis Method -- 3.2.3.6 Structure Refinement -- 3.3 Results -- 3.4 Discussion -- References -- Chapter 4: NMR Explorations of Biomolecular Systems with Rapid Conformational Exchanges -- 4.1 Introduction -- 4.2 Trapping Conformational States -- 4.2.1 High-Pressure NMR Combined with a Mutational Approach -- 4.2.2 Covalent Constraints of Biomolecular Conformations -- 4.3 Exploration of Conformational Spaces of Flexible Biomolecules -- 4.4 Concluding Remarks -- References -- Chapter 5: Site-Specific Incorporation of Fluorescent Nonnatural Amino Acids into Proteins and Its Application to Fluorescence... -- 5.1 Introduction -- 5.2 Incorporation of Nonnatural Amino Acids -- 5.3 Incorporation of Fluorescent Nonnatural Amino Acids -- 5.4 Application of Fluorescent Nonnatural Amino Acids to Protein Analysis -- 5.5 Synthesis of Fluorescent Protein Probes by Introducing Fluorescent Nonnatural Amino Acids -- 5.6 Antibody-Based Fluorescent Probes for Antigen Detection -- References -- Chapter 6: Unfoldomes and Unfoldomics: Introducing Intrinsically Disordered Proteins -- 6.1 Introducing Unfoldomes and Unfoldomics -- 6.2 Peculiarities of the Amino Acid Sequences of IDPs and IDPRs -- 6.3 Evaluation of Commonness of Disorder in Various Proteomes -- 6.4 Structural Heterogeneity of IDPs -- 6.5 Discovering and Characterizing the Disease-Related Unfoldomes -- 6.6 IDPs as Novel, Promising, but yet Inconvenient Drug Targets -- 6.7 Concluding Remarks -- References -- Chapter 7: Structure, Dynamics, and Function of Staphylococcal Nuclease -- 7.1 Introduction -- 7.2 Information Encoded in the Primary Structure -- 7.3 Mechanism of Induced Folding -- 7.4 Role of Nonlocal Interactions in Structure Formation -- 7.5 Conclusion.
,
References -- Chapter 8: Theory of Molecular Recognition and Structural Fluctuation of Biomolecules -- 8.1 Introduction -- 8.2 Statistical Mechanics of Molecular Recognition (3D-RISM/RISM) -- 8.3 Molecular Recognition and Drug Design -- 8.3.1 Water Molecules Bound in a Cavity of Lysozyme -- 8.3.2 Selective Ion Binding by Protein [9] -- 8.3.3 Binding of Aspirin to Phospholipase A2 (Application to Intelligent Drug Design) [24] -- 8.4 Structural Fluctuation of Protein and Molecular Recognition -- 8.4.1 Generalized Langevin Equation of a Protein-Solution System -- 8.5 Concluding Remarks -- References -- Chapter 9: Structural Fluctuations of Proteins in Folding and Ligand Docking Studied by Replica-Exchange Simulations -- 9.1 Introduction -- 9.2 Methods -- 9.2.1 Replica-Exchange Method -- 9.2.2 Multidimensional Replica-Exchange Method -- 9.3 Results -- 9.4 Conclusions -- References -- Chapter 10: Spatiotemporal Fluctuations of Protein Folding in Living Cells -- 10.1 Introduction -- 10.2 Protein Structure and Thermodynamics: Consequences of Environmental Modulation -- 10.3 Protein Folding, Binding, and Biological Function: Environmental Modulation of the Energy Landscape -- 10.4 Protein Binding and Function Fluctuate Within the Cell -- 10.5 Outlook -- References -- Chapter 11: Membrane-Targeted Nanotherapy with Hybrid Liposomes for Cancer Cells Leading to Apoptosis -- 11.1 Introduction -- 11.2 History of Hybrid Liposomes: Enzymological Application -- 11.3 Application for Drug Delivery System -- 11.4 Antitumor Effects In Vitro -- 11.5 Two Methylene Groups in Phospholipids Distinguish Between Apoptosis and Necrosis -- 11.6 Signaling Pathway for Apoptosis -- 11.7 Membrane Targeted Antitumor Mechanism -- 11.8 Therapeutic Effects and Toxicity In Vivo -- 11.9 Clinical Application -- 11.10 Conclusion -- References.
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Chapter 12: Antitumor Complexes Formed by Oleic Acid and Molten Globule Intermediates of Proteins -- 12.1 Introduction -- 12.2 Biological Functions and Physical Properties of α-Lactalbumin -- 12.3 HAMLET and Its Beneficial Properties -- 12.4 Preparation of HAMLET -- 12.5 Stoichiometry of Oleic Acid Binding to α-Lactalbumin -- 12.6 Is HAMLET Oligomeric or Monomeric? -- 12.7 Identification of the Oleic Acid-Binding Site in HAMLET and GAMLET -- 12.8 Antitumor Complexes Formed by Oleic Acid and Other Proteins in the Molten Globule State -- 12.9 Antitumor Complexes Formed by Other Unsaturated Fatty Acids and α-Lactalbumin -- 12.10 Conclusions -- References.
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