1 Step-wise Degradation of Peptides Attached to Solid Supports.- I. Introduction.- II. Choice of Solid Support.- III. Attachment of Peptides to Supports.- IV. Step-wise Degradation Procedures.- V. Automation of Solid Phase Degradation.- VI. Concluding Remarks.- 2 Coupling Methods and Strategies in Solid-Phase Sequencing.- I. Introduction.- II. Coupling Procedures.- III. Sequencing Strategies.- 3 Sequencing Peptides and Proteins Lacking Free ?-Amino Groups.- I. Introduction.- II. Isolation and Detection of Peptides Lacking Free ?-Amino Groups.- III. PCA-Terminating Peptides and Proteins.- IV. Acylated Peptides and Proteins.- V. Concluding Remarks.- 4 Use of Antibody in the Study of Protein Structure.- I. Introduction.- II. Measurement of the Ag-Ab Reaction.- III. The Effect of Conformational Changes on the Antigenicity of Proteins.- IV. Detection of Sequence Changes in Proteins with Antibodies.- V. Use of Antibody in the Study of Protein Evolution.- 5 Polarization of Light and Protein Structure.- I. Introduction.- II. Plane Polarized Light.- III. Circularly Polarized Light.- IV. Circular Dichroism.- V. Drude Equation.- VI. Optical Properties of Amino Acids.- VII. Optical Properties of Peptides.- VIII. Conclusion.- 6 The X-ray Crystallography Technique in Protein Sequencing.- I. Introduction.- II. Outline of the Protein Crystallographic Method.- III. Some Important Concepts in X-ray Diffraction Analysis of Protein Crystals.- IV. Building up the Electron Density Map.- V. Interpretation of the Electron Density Map.- VI. Correlation of the Chemical Sequence with the Electron Density Maps.- VII. Conclusion.- 7 Amino Acid Sequence Determination by Mass Spectrometry.- I. Introduction.- II. Instrumentation and Techniques.- III. Mass Spectrometry of Peptides.- IV. ConcludingRemarks.- 8 Peptide Sequence Analysis by Nuclear Magnetic Resonance Spectroscopy.- I. Introduction.- II. NMR Principles.- III. Amino Acid Composition and Residue Identification.- IV. Conclusions.- References.