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Protein Folding and Binding

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

Keywords

Gibbs Free Energy Molecular Chaperone Misfolded Protein Energy Landscape Denature State 
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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References and Further Reading

Anfinsen Nobel Prize Lecture

  1. Anfinsen CB [1973]. Principles that guide the folding of protein chains. Science, 181: 223–230.ADSCrossRefGoogle Scholar

Motions of Proteins

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  3. Forman-Kay JD [1999]. The “dynamics” in the thermodynamics of binding. Nature Struct. Biol., 6: 1086–1087.CrossRefGoogle Scholar
  4. Frauenfelder H, Sligar SG, and Wolynes PG [1991]. The energy landscapes and motions of proteins. Science, 254: 1598–1603.ADSCrossRefGoogle Scholar
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  6. Kern D, et al. [1999]. Structure of a transiently phosphorylated switch in bacterial signal transduction. Nature, 402: 894–898.CrossRefADSGoogle Scholar
  7. Lee AL, Kinnear SA, and Wand AJ [2000]. Redistribution and loss of side chain entropy upon formation of a calmodulin-peptide complex. Nature Struct. Biol., 7: 72–77.CrossRefGoogle Scholar
  8. Stock A [1999]. Relating dynamics to function. Nature, 400: 221–222.CrossRefADSGoogle Scholar
  9. Zidek L, Novotny MV, and Stone MJ [1999]. Increased protein backbone conformational entropy upon hydrophobic ligand binding. Nature Struct. Biol., 6: 1118–1121.CrossRefGoogle Scholar

Protein Folding: The Energy Landscape Picture

  1. Bryngelson JD, et al. [1995]. Funnels, pathways, and the energy landscape of protein folding: A synthesis. Proteins: Structure, Function and Genetics, 21: 167–195.CrossRefGoogle Scholar
  2. Chan HS, and Dill KA [1998]. Protein folding in the landscape perspective: Chevron plots and non-Arrhenius kinetics. Proteins: Structure, Function and Genetics, 30: 2–33.CrossRefGoogle Scholar
  3. Dill KA, and Chan HS [1997]. From Levinthal to pathways to funnels, Nature Structure Biology, 4: 10–19.zbMATHCrossRefGoogle Scholar
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  5. Onuchic JN, et al. [1995]. Toward an outline of the topography of a realistic protein-folding funnel. Proc. Natl. Acad. Sci. USA, 92: 3626–3630.CrossRefADSGoogle Scholar
  6. Sali A, Shakhnovich E, and Karplus M [1994]. How does a protein fold? Nature, 369: 248–251.CrossRefADSGoogle Scholar

Molecular Chaperones and Protein Folding in the Cell

  1. Hartl FU, and Hayer-Hartl M [2002]. Molecular chaperones in the cytosol: From nascent chain to folded proteins. Science, 295: 1852–1858.CrossRefADSGoogle Scholar
  2. Pratt WB [1998]. The Hsp90-based chaperone system: Involvement in signal transduction from a variety of hormone and growth factor receptors. Proc. Soc. Exp. Biol. Med., 217: 420–434.Google Scholar
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Binding Mechanisms

  1. DeLano WL, et al. [2000]. Convergent solutions to binding at a protein-protein interface. Science, 287: 1279–1283.CrossRefADSGoogle Scholar
  2. Freire E [1999]. The propagation of binding interactions to remote sites in proteins: Analysis of the binding of the monoclonal antibody D1.3 to lysozyme. Proc. Natl. Acad. Sci. USA, 96: 10118–10122.CrossRefADSGoogle Scholar
  3. Hilser VJ, et al. [1998]. The structural distribution of cooperative interactions in proteins: Analysis of the native state ensemble. Proc. Natl. Acad. Sci. USA, 95: 9903–9908.CrossRefADSGoogle Scholar
  4. Kumar S, et al. [2000]. Folding and binding cassettes: Dynamic landscapes and population shifts. Protein Sci., 9: 10–19.CrossRefGoogle Scholar
  5. Ma B, et al. [2002]. Multiple diverse ligands binding at a single protein site: A matter of pre-existing populations. Protein Sci., 11: 184–197.CrossRefGoogle Scholar
  6. Teague S [2003]. Implications of protein flexibility for drug design. Nature Rev. Drug Dis., 2: 527–541.CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media, Inc. 2005

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