Characterization of protein secondary structure from NMR chemical shifts

Steven P. Mielke, Viswanathan V Krishnan

Research output: Contribution to journalArticle

55 Scopus citations


Progress in the structural biology of proteins comes from both experimental and theoretical efforts. Computational methods are capable of delivering fast structural information, ranging from low-resolution protein structural class definition to high-quality information based on homology modeling. Experimental methods that concentrate on obtaining high-resolution information are hampered by inherent time cost, and lack the capacity to provide low-resolution structural information expediently. NMR spectroscopy is a powerful tool for obtaining high-resolution structural and dynamical details of molecules in the solution state. We have reviewed a number of semi-empirical methods for the fast identification of protein structures using NMR, emphasizing those that explore the degree to which chemical shifts of a particular nuclear species in the protein backbone can be used as a low-resolution parameter that correlates with a variety of important structural features.

Original languageEnglish (US)
Pages (from-to)141-165
Number of pages25
JournalProgress in Nuclear Magnetic Resonance Spectroscopy
Issue number3-4
StatePublished - Apr 5 2009


  • Chemical shift
  • Correlations
  • NMR
  • Protein
  • Secondary structure

ASJC Scopus subject areas

  • Analytical Chemistry
  • Spectroscopy
  • Nuclear and High Energy Physics
  • Materials Science(all)
  • Biochemistry

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