Conformation in Biology and Drug Design

The Peptides: Analysis, Synthesis, Biology, Vol. 7

1st Edition - November 26, 1985
Editors: Sidney Udenfriend, Johannes Meienhofer, Victor J. Hruby
Language: English
eBook ISBN:
9 7 8 - 1 - 4 8 3 2 - 1 8 0 0 - 7

The Peptides: Analysis, Synthesis, Biology, Volume 7: Conformation in Biology and Drug Design focuses on the analysis of peptides, emphasizing the use of physical methods in… Read more

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The Peptides: Analysis, Synthesis, Biology, Volume 7: Conformation in Biology and Drug Design focuses on the analysis of peptides, emphasizing the use of physical methods in peptide conformational analysis and the relationship of conformational properties of peptides to biological properties. This book consists of nine chapters. Chapter 1 provides a brief overview of the perspective on the application of physical methods to peptide conformational analysis. The use of circular dichroism (CD) spectroscopy to examine the conformational properties of peptides in solution is elaborated in Chapter 2, while the use of fluorescence spectroscopy to examine the special relationships of aromatic side-chain groups to one another is discussed in Chapter 3. In Chapter 4, the use of various theoretical methods to calculate the conformations of peptides is described. The methods used to stimulate peptide conformations and dynamics are outlined in Chapter 5. The last four chapters examine various aspects of the use of nuclear magnetic resonance (NMR) in peptide conformational analysis. This volume is suitable for biologists, specialists, and researchers interested in peptides and proteins.

Contributors

Preface

Nomenclature and Abbreviations

Chapter 1 A Perspective on the Application of Physical Methods to Peptide Conformational-Biological Activity Studies

I Introduction

II Some Biological Considerations

III Historical Development of Peptide Conformational Studies in Solution

IV Theoretical Methods for Examining Peptide Conformations

V Application of Conformational and Dynamic Studies of Peptides to Their Biological Activities

References

Chapter 2 Circular Dichroism of Peptides

I Introduction

II General Aspects of Peptide CD

III Specific Systems

References

Chapter 3 Application of Fluorescence Techniques in Studies of Peptide Conformations and Interactions

I Introductory Remarks

II Fluorophores in Peptides

III Fluorescence Quantum Yield and Lifetime Measurements

IV Fluorescence Polarization Studies

V Measurement of Intramolecular Distances by Singlet-Singlet Resonance Energy Transfer Experiments

VI Fluorescence Studies of Peptide Interactions with Macromolecular Systems

VII Concluding Remarks

References

Chapter 4 Theoretical Methods in the Analysis of Peptide Conformation

I Introduction

II Definitions and Conventions

III Methodology

IV Results

References

Chapter 5 Theoretical Simulation of Conformation, Energetics, and Dynamics of Peptides

I Introduction

II Techniques and Methodology

III Applications

IV Summary and Future Directions

References

Chapter 6 Paramagnetic Metal Ions as Nuclear Magnetic Resonance Probes of Peptide Conformation in Solution

I Introduction

II Paramagnetic Metal Ion-Induced Shifts and Relaxation Enhancements

III Conclusions

References

Chapter 7 Nuclear Magnetic Resonance Studies of Peptide-Macromolecule Interactions

I Introduction

II Nuclear Magnetic Resonance Techniques

III Peptide-Protein Interaction

IV Peptide-Lipid Interaction

V Peptide-Nucleic Acid Interactions

VI Conclusions and Prospects

References

Chapter 8 Solid-State Nuclear Magnetic Resonance of Peptides

I Introduction

II Methods

III Applications

IV Prospects

References

Chapter 9 Modern Nuclear Magnetic Resonance Spectroscopy of Peptides

I Introduction

II Conformational Homogeneity

III General Strategy for Nuclear Magnetic Resonance Investigation of Peptides

IV Assignment of Proton Nuclear Magnetic Resonance Signals

V Heteronuclear Techniques

VI Sequence Analysis

VII Quantitative Evaluation of Nuclear Magnetic Resonance Spectra

VIII Conclusions

References

Index