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Solid-State Deuterium NMR Spectroscopy of Membranes

  • Michael F. Brown
  • Silvia Lope-Piedrafita
  • Gary V. Martinez
  • Horia I. Petrache

Solid-state NMR spectroscopy is widely applicable to the investigation of non-crystalline or amorphous materials, e.g. polymers, glasses, protein precipitates, and membrane proteins. Rather than being mainly an alternative to X-ray crystallography, solid-state NMR is virtually unique among current analytical and spectroscopic methodologies in that it provides both structural and dynamical information at an atomically resolved level. In solid-state NMR, the structural information is obtained from the static or motionally averaged coupling tensors due to dipolar, chemical shift, or quadrupolar interactions [1,2]. Corresponding dynamical information is acquired from the tensor fluctuations, which depend on the mean-squared amplitudes and rates of the motions and affect the NMR lineshapes and relaxation times. For these reasons, solid-state NMR is finding increasing applicability in the chemistry of materials, structural biology, and genomics research, and this trend can be expected to continue well into the future.

Keywords

Acyl Chain Coupling Tensor Principal Axis System Quadrupolar Order Acyl Position 
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

© Springer 2008

Authors and Affiliations

  • Michael F. Brown
    • 1
    • 2
  • Silvia Lope-Piedrafita
    • 3
  • Gary V. Martinez
    • 1
  • Horia I. Petrache
    • 4
  1. 1.Department of ChemistryUniversity of ArizonaTucsonUSA
  2. 2.Department of PhysicsUniversity of ArizonaTucsonUSA
  3. 3.Department of RadiologyUniversity of ArizonaTucsonUSA
  4. 4.Laboratory of Physical and Structural BiologyNational Institutes of Health, NICHDBethesdaUSA

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