Dynamic activation of protein function: A view emerging from NMR spectroscopy

@article{Wand2001DynamicAO,
  title={Dynamic activation of protein function: A view emerging from NMR spectroscopy},
  author={A Joshua Wand},
  journal={Nature Structural Biology},
  year={2001},
  volume={8},
  pages={926-931}
}
Recent developments in solution NMR methods have allowed for an unprecedented view of protein dynamics. Current insights into the nature of protein dynamics and their potential influence on protein structure, stability and function are reviewed. Particular emphasis is placed on the potential of fast side chain motion to report on the residual conformational entropy of proteins and how this entropy can enter into both the thermodynamic and kinetic aspects of protein function. 
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Dynamics of a de novo designed threehelix bundle protein studied by 15 N , 13 C , and 2 H NMR relaxation methods

S. T. R. Walsh, A. L. Lee, W. F. De Grado, A. J. Wand
  • Biochemistry
  • 2001

Dynamics of a de novo designed threehelix bundle protein studied by 15 N , 13 C , and 2 H NMR relaxation methods

S. T. R. Walsh, A. L. Lee, W. F. De Grado, A. J. Wand
  • Biochemistry
  • 2001