title: Fast real-time NMR methods for characterizing short-lived molecular states.
abstract: The characterization of both the structure and the conformational dynamics of biological macromolecules, namely proteins and nucleic acids, is required for understanding the molecular mechanisms underlying physiological function and disease. Molecular dynamics involves the transient departure from the ground-state structures to populate short-lived excited state conformations that can play important functional roles. Real-time multi-dimensional NMR spectroscopy represents a unique tool for investigating dynamic molecular processes occurring on time scales of seconds or longer, providing atomic-resolution information about short-lived states. In this minireview, we discuss recent progress made in the field of fast real-time multidimensional NMR. The potential of these new methods is illustrated for several biomolecular systems that have recently been studied by fast real-time multidimensional NMR.
authors.affiliation: Biomolecular NMR spectroscopy group Institut de Biologie Structurale, Université Grenoble 1, CNRS, CEA, 41, rue Jules Horowitz, 38027 Grenoble Cedex 1 (France), Fax: (+33) 4 38 78 54 94.
authors.forename: Enrico
authors.initials: E
authors.lastname: Rennella
authors.forename: Bernhard
authors.initials: B
authors.lastname: Brutscher
mesh_terms: D004194:Disease; D006801:Humans; D007768:Lactalbumin / Q000737:chemistry; D008024:Ligands; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D009696:Nucleic Acids / Q000737:chemistry*; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*
chemical_list: D008024:Ligands; D009696:Nucleic Acids; D011506:Proteins; D007768:Lactalbumin
keywords: RNA switches; energy landscapes; fast multidimensional nmr spectroscopy; protein folding; real-time nmr spectroscopy