Exploring Protein Structure and Function

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


Nuclear Magnetic Resonance Circular Dichroism Protein Data Bank Electromagnetic Radiation Fluorescence Resonance Energy Transfer 
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Books on Protein Structure, X-Ray Crystallography, and NMR

  1. Brandon C, and Tooze J [1999]. Introduction to Protein Structure, 2nd edition. New York: Garland Science Publishing.Google Scholar
  2. Drenth J [1998]. Principles of Protein X-ray Crystallography. New York: Springer-Verlag.Google Scholar
  3. Hore PJ [1995]. Nuclear Magnetic Resonance. Oxford: Oxford University Press.Google Scholar
  4. Levitt MH [2001]. Spin Dynamics: Basics of Nuclear Magnetic Resonance. New York: John Wiley and Sons.Google Scholar
  5. Rhodes G [2000]. Crystallography Made Crystal Clear: A Guide for Users of Macromolecular Models, 2nd edition. San Diego: Academic Press.Google Scholar
  6. Woolfson MM [2001]. An Introduction to X-ray Crystallography. Cambridge: Cambridge University Press.Google Scholar

References and Further Reading X-Ray Crystallography, Electron Crystallography, and NMR

  1. Campbell ID, and Downing AK [1998]. NMR of modular proteins. Nat. Struct. Biol. (Suppl.), 5: 496–499.CrossRefGoogle Scholar
  2. Kühlbrandt W, and Wang DN [1991]. Three-dimensional structure of plant light-harvesting complex determined by electron crystallography. Nature, 350: 130–134.CrossRefADSGoogle Scholar
  3. Unwin N [1993]. Nicotinic acetylcholine receptor at 9 Å resolution. J. Mol. Biol., 229: 1101–1124.CrossRefGoogle Scholar
  4. Unwin N [1995]. Acetylcholine receptor channel imaged in the open state. Nature, 373: 37–43.CrossRefADSGoogle Scholar
  5. Wilson KS [1998]. Illuminating crystallography. Nat. Struct. Biol. (Suppl.), 5: 627–630.CrossRefGoogle Scholar

Fluorescence Resonance Energy Transfer

  1. Bastiaens PIH, and Pepperkok R [2000]. Observing proteins in their natural habitat: The living cell. Trends Biochem. Sci., 25: 631–637.CrossRefGoogle Scholar
  2. Matz MV, et al. [1999]. Fluorescent proteins from nonbioluminescent Anthozoa species. Nat. Biotechnol., 17: 969–973.CrossRefGoogle Scholar
  3. Pollok BA, and Heim R [1999]. Using GFP in FRET-based applications. Trends in Cell Biol., 9: 57–60.CrossRefGoogle Scholar
  4. Weiss S [1999]. Fluorescence spectroscopy of single biomolecules. Science, 283: 1676–1683.CrossRefADSGoogle Scholar

Circular Dichroism

  1. Johnson WC [1990]. Protein secondary structure and circular dichroism: A practical guide. Proteins, 7: 205–214.CrossRefGoogle Scholar
  2. Woody RW [1995]. Circular dichroism. Methods in Enzymology, 246: 34–71.CrossRefGoogle Scholar

Yeast Two-Hybrid System

  1. Chien CT, et al. [1991]. The two-hybrid system: A method to identify and clone genes for proteins that interact with a protein of interest. Proc. Natl. Acad. Sci. USA, 88: 9578–9582.CrossRefADSGoogle Scholar
  2. Finley RL, Jr., and Brent R [1994]. Interaction mating reveals binary and ternary connections between Drosophila cell cycle regulators. Proc. Natl. Acad. Sci. USA, 91: 12980–12984.CrossRefADSGoogle Scholar
  3. Ito T, et al. [2001]. A comprehensive two-hybrid analysis to explore the yeast protein interactome. Proc. Natl. Acad. Sci. USA, 98: 4569–4574.CrossRefADSGoogle Scholar
  4. Uetz P, et al. [2000]. A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae. Nature, 403: 623–627.CrossRefADSGoogle Scholar
  5. Walhout AJM, et al. [2000]. Protein interaction mapping in C. elegans using proteins involved in vulval development. Science, 287: 116–122.CrossRefADSGoogle Scholar

2D Gel Electrophoresis

  1. Gygi SP, et al. [1999]. Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat. Biotechnol., 17: 994–999.CrossRefGoogle Scholar

Mass Spectrometry

  1. Link AJ, et al. [1999]. Direct analysis of protein complexes using mass spectrometry, Nat. Biotechnol., 17: 676–682.CrossRefGoogle Scholar
  2. Yates JR, 3rd [1998]. Mass spectrometry and the age of the proteome. J. Mass Spectrom., 33: 1–19.CrossRefGoogle Scholar

Gene Fusion, Gene Expression Profiles, and Combined Methods

  1. Enright AJ, et al. [1999]. Protein interaction maps for complete genomes based on gene fusion events. Nature, 402: 86–90.CrossRefADSGoogle Scholar
  2. Lockhart DJ, and Winzeler EA [2000]. Genomics, gene expression and DNA arrays. Nature, 405: 827–836.CrossRefGoogle Scholar
  3. Marcotte EM, et al. [1999a]. Detecting protein function and protein-protein interactions from genome sequences. Science, 285: 751–753.CrossRefGoogle Scholar
  4. Marcotte EM, et al. [1999b]. A combined algorithm for genome-wide prediction of protein function. Nature, 402: 83–86.CrossRefADSGoogle Scholar
  5. Pellegrini M, et al. [1999]. Assigning protein functions by comparative genome analysis: Protein phylogenetic profiles. Proc. Natl. Acad. Sci. USA, 96: 4285–4288.CrossRefADSGoogle Scholar
  6. Schwekowski B, Uetz P, and Fields S [2000]. A network of protein-protein interactions in yeast. Nat. Biotechnol., 18: 1257–1261.CrossRefGoogle Scholar
  7. Young RA [2000]. Biomedical discovery with DNA arrays. Cell, 102: 9–15.CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media, Inc. 2005

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