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Macromolecular Forces

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Part of the Biological and Medical Physics, Biomedical Engineering book series (BIOMEDICAL)

Keywords

Salt Bridge Atomic Radius Electron Cloud Protein Interface Bond Axis 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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General Reference

  1. Brandon C, and Tooze J [1999]. Introduction to Protein Structure, 2nd edition. New York: Garland Science Publishing.Google Scholar

References and Further Reading Physical and Electrostatic Properties of Amino Acids and Proteins

  1. Bolen DW, and Baskakov IV [2001]. The osmophobic effect: Natural selection of a thermodynamic force in protein folding. J. Mol. Biol., 310: 955–963.CrossRefGoogle Scholar
  2. Dill KA [1990]. Dominant forces in protein folding. Biochem., 29: 7133–7155.CrossRefGoogle Scholar
  3. Myers JK, and Pace CN [1996]. Hydrogen bonding stabilizes globular proteins. Biophys. J., 71: 2033–2039.CrossRefADSGoogle Scholar
  4. Pace CN, et al. [1996]. Forces contributing to the conformational stability of proteins. FASEB J., 10: 75–83.Google Scholar
  5. Sheinerman FB, and Honig B [2002]. On the role of electrostatic interactions in the design of protein-protein interfaces. J. Mol. Biol., 318: 161–177.CrossRefGoogle Scholar
  6. Tsai J, et al. [1999]. The packing density in proteins: Standard radii and volumes. J. Mol. Biol., 290: 253–266.CrossRefGoogle Scholar

Complementarity and Interfaces

  1. Glaser F, et al. [2001]. Residue frequencies and pairing preferences at proteinprotein interfaces. Proteins, 43: 89–102.CrossRefGoogle Scholar
  2. Lo Conte L, Chothia C, and Janin J [1999]. The atomic structure of protein-protein recognition sites. J. Mol. Biol., 285: 2177–2198.CrossRefGoogle Scholar
  3. Jones S, and Thornton JM [1996]. Principles of protein-protein interactions. Proc. Natl. Acad. Sci. USA, 93: 13–20.CrossRefADSGoogle Scholar
  4. Jones S, et al. [1999]. Protein-DNA interactions: A structural analysis. J. Mol. Biol., 287: 877–896.CrossRefGoogle Scholar
  5. Nadassy K, Wodak SJ, and Janin J [1999]. Structural features of protein-nucleic acid recognition sites. Biochem., 38: 1999–2017.CrossRefGoogle Scholar
  6. Norel R, et al. [1999]. Examination of shape complementarity in docking of unbound proteins. Proteins, 36: 307–317.CrossRefGoogle Scholar
  7. Sheinerman FB, Norel R, and Honig B [2000]. Electrostatic aspects of proteinprotein interactions. Curr. Opin. Struct. Biol., 10: 153–159.CrossRefGoogle Scholar

Hot Spots

  1. Bogan AA, and Thorn KS [1998]. Anatomy of hot spots in protein interfaces. J. Mol. Biol., 280: 1–9.CrossRefGoogle Scholar
  2. Hu ZJ, et al. [2000]. Conservation of polar residues as hot spots at protein interfaces. Proteins, 39: 331–342.CrossRefGoogle Scholar

Theoretical Methods: Computer Modeling and Simulation

  1. Cornell WD, et al. [1995]. A second generation force field for the simulation of proteins, nucleic acids, and organic molecules. J. Am. Chem. Soc., 117: 5179–5197.CrossRefGoogle Scholar
  2. Elcock AH, Sept D, and McCammon JA [2001]. Computer simulation of proteinprotein interactions. J. Phys. Chem. B, 105: 1504–1518.CrossRefGoogle Scholar
  3. Honig B, and Nicholls A [1995]. Classical electrostatics in biology and chemistry. Science, 268: 1144–1149.ADSCrossRefGoogle Scholar
  4. Kollman PA, et al. [2000]. Calculating structures and free energies of complex molecules: Combining molecular mechanics and continuum models. Acc. Chem. Res., 33: 889–897.CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media, Inc. 2005

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