Characterization of protein secondary structure from NMR chemical shifts

Steven P. Mielke, Viswanathan V Krishnan

Research output: Contribution to journalArticlepeer-review

69 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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