About the Book
Please note that the content of this book primarily consists of articles available from Wikipedia or other free sources online. Pages: 158. Chapters: Disulfide bond, X-ray crystallography, Structural biology, Protein secondary structure, Protein Data Bank, Protein folding, Circular dichroism, Protein tertiary structure, Protein primary structure, Ubiquitin, Denaturation, Globular protein, Integral membrane protein, Protein quaternary structure, Posttranslational modification, Molten globule, Protein domain, Cyclol, Folding@home, Rosetta@home, Protein structure prediction, Homology modeling, Implicit solvation, Protein nuclear magnetic resonance spectroscopy, Macromolecular docking, Protein Structure Initiative, Electron crystallography, Residual dipolar coupling, Protein design, Statistical potential, Equilibrium unfolding, Intrinsically unstructured proteins, Pore-forming toxin, Phosphatase, Downhill folding, Beta barrel, CARD domain, Hydrogen-deuterium exchange, Single particle analysis, RNA polymerase II holoenzyme stability, Ribbon diagram, Dihedral angle, Fiber diffraction, Iron-sulfur protein, List of protein structure prediction software, Phi value analysis, Scoring functions for docking, Polyhistidine-tag, Protein crystallization, Protein fragment library, InterPro, Accessible surface area, Oxidative folding, Arthur M. Lesk, Searching the conformational space for docking, HB plot, Chevron plot, Capping enzyme complex, Cryo-electron microscopy, BZIP domain, Zimm-Bragg model, Levinthal's paradox, Magnetic resonance force microscopy, Conserved sequence, Lifson-Roig model, Structural Classification of Proteins, Foldit, Anfinsen's dogma, CING, N-terminus, MWC model, WHAT IF software, C-terminus, WW domain, Structural motif, Lattice protein, Guanidinium chloride, Contact order, De novo protein structure prediction, CATH, Conformational entropy, Half sphere exposure, Citrullination, Protein contact map, Edman degradation, Loop modeling, Residue depth, ..
