Determination of three-dimensional structure

Clore, G.M., Gronenborn, A.M. Determination of three-dimensional structures of proteins and nucleic acids in solution by nuclear magetic resonance spectroscopy. CRC Crit. Rev. Biochem. 24 479-564, 1989. 

Hendrickson WA, Horton JR, LeMaster DM. Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD) a vehicle for direct determination of three-dimensional structure. EMBO J... 

A coirplete understanding of the role of carbohydrates in biological systems requires knowledge of the distribution at equilibrium of the various conformers in aqueous solution. The conformational behavior of carbohydrates in solution can be examined from different vantage points (1,), but the most relevant approach is, no doubt, study of dilute solutions themselves. At present, high resolution NMR spectroscopy is the primary tool for determination of three-dimensional structure of oligosaccharides in solution. Optical rotation is also very sensitive to conformation (2) and there is a new, semi-enqpirical theory of optical rotation of oligosaccharides ( ). 

Until now, the determination of three-dimensional structures of oligosaccharides in solution was based primarily on proton-proton distance information obtained from n.O.e. data. Here, we discuss the application of three-bond proton-carbon coupling constants. 

Smith, J. L. (1991). Determination of three-dimensional structure by multiwavelength anomalous diffraction. Current Opin. Struct. Biol 1,1002-1011. 

M. Nilges, A. M. Gronenborn, A. T. Brunger, and G. M. Clore, Protein Engin., 2,27 (1988). Determination of Three-Dimensional Structures of Proteins by Simulated Annealing with Interproton Distance Restraints. Application to Crambin, Potato Carboxypeptidase Inhibitor, and Barley Serine Proteinase Inhibitor 2. 

Determination of Three-Dimensional Structures of Nucleic Acids by NMR... 

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