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Determination of Structural Uncertainty from NMR and Other Data: The Lac Repressor Headpiece

  • Russ B. Altman
  • Ruth Pachter
  • Oleg Jardetzky
Part of the NATO ASI Series book series (NSSA, volume 183)

Abstract

The static high resolution structures determined by x-ray crystallography have provided most of our structural information about protein structure (Blundell and Johnson, 1972). While these structures have provided a wealth of data about common motifs and folding patterns within proteins, there remains an important unresolved issue: is the set of crystallizable proteins representative of all proteins, or are we necessarily seeing a biased sample whose motifs and folding patterns are themselves part of the necessary determinants for crystallization? It is possible, perhaps likely, that there are important protein structural motifs that have not been observed in crystalline structures precisely because the properties of the motif s (for example, in the lac-repressor the high degree of hinge motion (Pilz et al., 1980) makes crystallization difficult or impossible. These considerations have lead many investigators to techniques such as high resolution NMR spectroscopy to study the structures of proteins in solution (for summaries, see Jardetzky and Roberts, 1981; Wiithrich, 1986). It is hoped that these studies will furnish complementary data about the structure and dynamics of proteins.

Keywords

Secondary Structure Root Mean Square Backbone Atom Distance Constraint Bloch Equation 
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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Copyright information

© Plenum Press, New York 1989

Authors and Affiliations

  • Russ B. Altman
    • 1
  • Ruth Pachter
    • 1
  • Oleg Jardetzky
    • 1
  1. 1.Stanford Magnetic Resonance LaboratoryStanford University Medical CenterStanfordUSA

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