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NMR contributions to structural dynamics studies of intrinsically disordered proteins.

ABSTRACT: Intrinsically disordered proteins (IDPs) are characterized by substantial conformational plasticity. Given their inherent structural flexibility X-ray crystallography is not applicable to study these proteins. In contrast, NMR spectroscopy offers unique opportunities for structural and dynamic studies of IDPs. The past two decades have witnessed significant development of NMR spectroscopy that couples advances in spin physics and chemistry with a broad range of applications. This article will summarize key advances in basic physical-chemistry and NMR methodology, outline their limitations and envision future R&D directions.

SUBMITTER: Konrat R

PROVIDER: S-EPMC3985426 | biostudies-literature | 2014 Apr

REPOSITORIES: biostudies-literature

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NMR contributions to structural dynamics studies of intrinsically disordered proteins.

Konrat Robert R

Journal of magnetic resonance (San Diego, Calif. : 1997) 20140401

Intrinsically disordered proteins (IDPs) are characterized by substantial conformational plasticity. Given their inherent structural flexibility X-ray crystallography is not applicable to study these proteins. In contrast, NMR spectroscopy offers unique opportunities for structural and dynamic studies of IDPs. The past two decades have witnessed significant development of NMR spectroscopy that couples advances in spin physics and chemistry with a broad range of applications. This article will su ...[more]

PMID: 24656082

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