Protein Folding and Binding

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


Gibbs Free Energy Molecular Chaperone Misfolded Protein Energy Landscape Denature State 
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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

  1. Cavanagh J, and Akke M [2000]. May the driving force be with you—Whatever it is. Nature Struct. Biol., 7: 11–13.CrossRefGoogle Scholar
  2. Feher VA, and Cavanagh J [1999]. Millisecond-timescale motions contribute to the function of the bacterial response regulator protein Spo0F. Nature, 400: 289–293.CrossRefADSGoogle Scholar
  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
  5. Kay LE, et al. [1996]. Correlation between dynamics and high affinity binding in an SH2 domain interaction. Biochem., 35: 361–368.CrossRefGoogle Scholar
  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
  4. Leopold PE, Montal M, and Onuchic JN [1992]. Protein folding funnels: A kinetic approach to the sequence-structure relationship. Proc. Natl. Acad. Sci. USA, 89: 8721–8725.CrossRefADSGoogle Scholar
  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
  3. Rutherford SL, and Lindquist S [1998]. Hsp90 as a capacitor for morphological evolution. Nature, 396: 226–342.CrossRefGoogle Scholar
  4. Sauer FG, et al. [2000]. Chaperone-assisted pilus assembly and bacterial attachment. Curr. Opin. Struct. Biol., 10: 548–556.CrossRefGoogle Scholar

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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