Water and biomolecules : physical chemistry of life phenomena

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Water and biomolecules : physical chemistry of life phenomena / Kunihiro Kuwajima ... [et al.] (eds.)

資料種別:

電子ブック

出版情報:

Berlin : Springer, c2009

形態:

1 online resource

シリーズ名:

Biological and medical physics, biomedical engineering <BA67747899>

著者名:

ISBN:

9783540887867 [3540887865]
9783540887874 [3540887873] (: online)

書誌ID:

TT00015689

子書誌情報

フルテキスト

所蔵情報

書誌詳細

注記:

Includes bibliographycal references and index

著者名ヨミ:

クワジマ, クニヒロ
ゴトウ, ユウジ
ヒラタ, フミオ
テラジマ, マサヒデ

主題:

分子生物学．放射線生物学

言語:

英語

目次情報:

Mapping Protein Folding Landscapes by NMR Relaxation / P.E. Wright ; D.J. Felitsky ; K. Sugase ; H.J. Dyson1：

NMR Techniques for Studying Protein Folding / 1.1：

The Apomyoglobin Folding Landscape / 1.2：

Structure of the Kinetic Molten Globule State / 1.3：

The Upper Reaches of the Folding Landscape / 1.4：

Paramagnetic Relaxation Probes: Spin Labeling of Apomyoglobin / 1.5：

Model for Transient Interactions / 1.6：

Information from Relaxation Dispersion Measurements / 1.7：

Folding of an Intrinsically Disordered Protein Upon Binding to a Target / 1.8：

References

Experimental and Simulation Studies of the Folding/Unfolding of Goat ?-Lactalbumin / K. Kuwajima ; T. Oroguchi ; T. Nakamura ; M. Ikeguchi ; A. Kidera2：

Introduction / 2.1：

Goat ?-Lactalbumin / 2.2：

Differences Between the Unfolding Behaviors of Authentic and Recombinant Goat ?-Lactalbumin / 2.3：

Experimental Studies / 2.3.1：

Simulation Studies / 2.3.2：

Conclusions / 2.3.3：

Folding/Unfolding Pathways of Goat ?-Lactalbumin / 2.4：

Summary and Perspectives / 2.4.1：

Transition in the Higher-order Structure of DNA in Aqueous Solution / T. Sakaue ; K. Yoshikawa3：

Long DNA Molecules in Aqueous Solution / 3.1：

Primary, Secondary, and Higher-order Structures / 3.2.1：

DNA Condensation / 3.2.2：

Looking at Single DNA Molecules / 3.2.3：

Statistical Physics of Folding of a Long Polymer / 3.3：

Some Basis / 3.3.1：

Continuous Transition in Flexible Polymers: Coil-Globule Transition / 3.3.2：

Discontinuous Transition in Semiflexible Polymers / 3.3.3：

Instability Due to the Remanent Charge / 3.3.4：

Higher-order Structure and Genetic Activity / 3.4：

Toward Chromatin Structure / 3.4.2：

Generalized-Ensemble Algorithms for Studying Protein Folding / Y. Okamoto4：

Generalized-Ensemble Algorithms / 4.1：

Multicanonical Algorithm / 4.2.1：

Multidimensional Extensions of Multicanonical Algorithm / 4.3：

Replica-Exchange Method / 4.3.1：

Multidimensional Extensions of Replica-Exchange Method / 4.3.2：

Examples of Simulation Results / 4.4：

Protein Folding and Binding: Effective Potentials, Replica Exchange Simulations, and Network Models / A.K. Felts ; M. Andrec ; E. Gallicchio ; R.M. Levy4.5：

Methods / 5.1：

The OPLS-AA/AGBNP Effective Potential / 5.2.1：

Replica Exchange Molecular Dynamics / 5.2.2：

The Network Model of Protein Folding / 5.2.3：

Loop Prediction with Torsion Angle Sampling / 5.2.4：

Folding of Peptides / 5.3：

G-Peptide Folding / 5.3.1：

Folding of Other Small Peptides / 5.3.2：

Loop Prediction / 5.3.3：

Kinetic Model of the G-Peptide / 5.4：

The G-Peptide has Apparent Two-State Kinetics After a Small Temperature Jump Perturbation / 5.4.1：

The G-Peptide has an ?-Helical Intermediate During Folding from Coil Conformations / 5.4.2：

A Molecular View of Kinetic Pathways / 5.4.3：

Ligand Conformational Equilibrium in a Cytochrome P450 Complex / 5.5：

Methodology / 5.5.1：

The Population of the Proximal State as a Function of Temperature / 5.5.2：

Simple Continuous and Discrete Models for Simulating Replica Exchange / 5.6：

Discrete Network Replica Exchange (NRE) / 5.6.1：

RE Simulations using MC on a Continuous Potential / 5.6.2：

Conclusion / 5.7：

Functional Unfolded Proteins: How, When, Where, and Why? / S.-C. Sue6：

What is a Functional Unfolded Protein? / 6.1：

Where do Functional Unfolded Proteins Occur? / 6.2：

How Are Functional Unfolded Proteins Studied? / 6.3：

NMR Spectra: Practical Considerations / 6.4：

Dynamic Complexes in CBP / 6.5：

Role of Flexibility in the Function of I$$B? / 6.6：

Structure of the Photointermediate of Photoactive Yellow Protein and the Propagation Mechanism of Structural Change / M. Kataoka ; H. Kamikubo7：

Solution X-ray Scattering / 7.1：

Photoactive Yellow Protein / 7.2：

Solution Structure Analysis of Photointermediate of PYP / 7.3：

High-Angle X-ray Scattering of PYP in the Dark and in the Light / 7.3.1：

Analysis of High Angle Scattering / 7.3.2：

Propagation Mechanism of the Structural Change / 7.4：

Summary / 7.5：

Time-Resolved Detection of Intermolecular Interaction of Photosensor Proteins / M. Terazima8：

Principle / 8.1：

Diffusion Coefficient / 8.3：

Time-Resolved Detection of Interprotein Interactions / 8.4：

Protein-Protein Interaction of the Photoexcited Photoactive Yellow Protein / 8.4.1：

Photoinduced Dimerization of AppA / 8.4.2：

Photoinduced Dimerization and Dissociation of Phototropins / 8.4.3：

Diffusion Detection of Interprotein Interaction / 8.4.4：

Volumetric Properties of Proteins and the Role of Solvent in Conformational Dynamics / C.A. Royer ; R. Winter9：

Thermodynamics / 9.1：

Thermal Expansivity and ?V / 9.3：

A Statistical Mechanics Theory of Molecular Recognition / T. Imai ; N. Yoshida ; A. Kovalenko ; F. Hirata9.4：

Outline of the RISM and 3D-RISM Theories / 10.1：

Recognition of Water Molecules by Protein / 10.3：

Noble Gas Binding to Protein / 10.4：

Selective Ion-Binding by Protein / 10.5：

Pressure-Induced Structural Transition of Protein and Molecular Recognition / 10.6：

Perspective / 10.7：

Computational Studies of Protein Dynamics / J.A. McCammon11：

Brief Survey of Protein Motions / 11.1：

Binding and Selectivity / 11.3：

Concerted Binding and Release / 11.4：

Molecular Clocks / 11.5：

Biological Functions of Trehalose as a Substitute for Water / M. Sakurai12：

Hydration Property of Trehalose / 12.1：

Property of the Aqueous Solution of Trehalose / 12.2.1：

Atomic-Level Picture of Hydration of Trehalose / 12.2.2：

Solid-State Property of Trehalose / 12.3：

Polymorphism / 12.3.1：

Glassy State of Trehalose / 12.3.2：

Biological Roles of Trehalose / 12.4：

Possible Mechanisms of Anhydrobiosis / 12.4.1：

Strategy for Desiccation Tolerance in the Sleeping Chironomid / 12.4.2：

Other Biological Roles of Trehalose / 12.4.3：

Protein Misfolding Diseases and the Key Role Played by the Interactions of Polypeptides with Water / C.M. Dobson12.5：

The Importance of Normal and Aberrant Protein Folding in Biology / 13.1：

Protein Aggregation and Amyloid Formation / 13.3：

Molecular Evolution and the Control of Protein Misfolding / 13.4：

Impaired Misfolding Control and the Onset of Disease / 13.5：

Probing Misfolding and Aggregation in Living Organisms / 13.6：

The Recent Proliferation of Misfolding Diseases and Prospects for Effective Therapies / 13.7：

Concluding Remarks / 13.8：

Effect of UV Light on Amyloidogenic Proteins: Nucleation and Fibril Extension / A.K. Thakur ; Ch. Mohan Rao14：

Amyloid / 14.1：

Structural Perturbation / 14.2.1：

Nucleation / 14.2.2：

Fibril Extension / 14.2.3：

UV Light as a Potent Structural Perturbant / 14.3：

UV-Induced Aggregation of Prion Protein / 14.3.1：

Prevention of UV-Induced Aggregation of Prion Protein / 14.3.2：

UV Exposure Alters Conformation of Prion Protein / 14.3.3：

UV-Exposed Proteins Failed to Form Amyloid De Novo / 14.3.4：

Is Subcritical Concentration of UV-Exposed Protein Responsible for Failure to Form Amyloid Fibrils? / 14.3.5：

UV-Exposed Amyloidogenic Proteins Form Amyloid Upon Seeding / 14.3.6：

UV-Exposed Prion Protein Fibrils Show Altered Fibril Morphology / 14.3.7：

Discussion / 14.4：

Real-Time Observation of Amyloid Fibril Growth by Total Internal Reflection Fluorescence Microscopy / H. Yagi ; T. Ban ; Y. Goto15：

Total Internal Reflection Fluorscence Microscopy / 15.1：

Real-Time Observation of ?2-m and A? Fibrils / 15.3：

Effects of Various Surfaces on the Growth of A? Fibrils / 15.4：

Spontaneous Formation of A?(1-40) Fibrils and Classification of Morphologies / 15.5：

Index / 15.6：

Mapping Protein Folding Landscapes by NMR Relaxation / P.E. Wright ; D.J. Felitsky ; K. Sugase ; H.J. Dyson1：

NMR Techniques for Studying Protein Folding / 1.1：

The Apomyoglobin Folding Landscape / 1.2：

Structure of the Kinetic Molten Globule State / 1.3：

The Upper Reaches of the Folding Landscape / 1.4：

Paramagnetic Relaxation Probes: Spin Labeling of Apomyoglobin / 1.5：

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