Protein Structure and Engineering: NATO Science Series A:, cartea 183

X-Ray.- Exploitation of Geometric Redundancies as a Source of Phase Information in X-ray Structure Analysis of Symmetric Protein Assemblies.- Escherichia Coli Aspartate Transcarbamylase: the Relationship Between Structure and Function.- Fundamentals of Neutron Diffraction.- Purification of Complexes Between Peptide Antigens and Class II Major Histocompatibility Complex Antigens Using Biotinylated Peptides.- Nuclear Magnetic Resonance.- NMR Method for Protein Structure Determination in Solution.- Determination of Structural Uncertainty from NMR and Other Data: The Lac Repressor Headpiece.- The Generation of Three-Dimensional Structures from NMR-Derived Constraints.- 2D-NMR for 3D-Structure of Membrane Spanning Polypeptides: Gramacidin A and Fragments of Bacteriorhodopsin.- The Dynamics of Oligonucleotides and Peptides Determined by Proton NMR.- Methods of Stable-Isotope-Assisted Protein NMR Spectroscopy in Solution.- NMR Studies of Protein Dynamics and Folding.- Understanding the Specificity of the Dihydrofolate Reductase Binding Site.- Histone H1 Solution Structure and the Sealing of Mammalian Nucleosome.- 1H NMR Studies of Genetic Variants and Point Mutants of Myoglobin: Modulation of Distal Steric Tilt of Bound Cyanide Ligand.- Molecular Dynamics.- Spectroscopy of Molecular Structure and Dynamics.- Molecular Dynamics: Applications to Proteins.- Site-Directed Mutagenesis.- Protein Engineering and Biophysical Studies of Metal Binding Proteins.- Growth Hormones: Expression, Structure and Protein Engineering.- Cloning, Sequencing and Expression of a New ?-Galactosidase from the Extreme Thermophilic Sulfolobus Solfataricus.- Site-Directed Mutagenesis and the Mechanism of Flavoprotein Disulphide Oxidoreductases.- Resonance Raman and Site-Directed Mutagenesis Studies ofMyoglobin Dynamics.- Comparison of the Secondary Structures of Human Class I and Class II MHC Antigens by FTIR and CD Spectroscopy.- Specificities of Germ Line Antibodies.- Contributors.