Literature DB >> 21404360

NMR reveals novel mechanisms of protein activity regulation.

Charalampos G Kalodimos1.   

Abstract

NMR spectroscopy is one of the most powerful tools for the characterization of biomolecular systems. A unique aspect of NMR is its capacity to provide an integrated insight into both the structure and intrinsic dynamics of biomolecules. In addition, NMR can provide site-resolved information about the conformation entropy of binding, as well as about energetically excited conformational states. Recent advances have enabled the application of NMR for the characterization of supramolecular systems. A summary of mechanisms underpinning protein activity regulation revealed by the application of NMR spectroscopy in a number of biological systems studied in the lab is provided.
Copyright © 2011 The Protein Society.

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Year:  2011        PMID： 21404360      PMCID： PMC3125862          DOI： 10.1002/pro.614

Source DB:  PubMed          Journal:  Protein Sci        ISSN： 0961-8368            Impact factor:   6.725


  105 in total

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4.  Structure of dimeric SecA, the Escherichia coli preprotein translocase motor.

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Review 4.  NMR and computational methods for molecular resolution of allosteric pathways in enzyme complexes.

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6.  Determination of structural fluctuations of proteins from structure-based calculations of residual dipolar couplings.

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7.  The feasibility of parameterizing four-state equilibria using relaxation dispersion measurements.

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Review 8.  New opportunities for tensor-free calculations of residual dipolar couplings for the study of protein dynamics.

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9.  Structures of the excited states of phospholamban and shifts in their populations upon phosphorylation.

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