Comparison of protein structures by high resolution solid state and solution NMR
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Comparisons of the crystal and solution structure of proteins are usually based on circumstantial evidence. Direct structure determination is possible only in the solid state, and to make the comparison, various spectroscopic findings (CD, ORD, NMR), or results of chemical modification experiments are tested for consistency with the known crystal structure [ 11. To be rigorous a comparison should be based on data obtained by the same method on the same object under two different conditions. Here we present an experiment which makes such a direct comparison of the crystal and solution structure of proteins by high resolution “C NMR.
[1] O. Jardetzky,et al. Nuclear magnetic resonance studies of the structure and binding sites of enzymes. II. Spectral assignments and inhibitor binding in hen egg-white lysozyme. , 1968, Proceedings of the National Academy of Sciences of the United States of America.
[2] O. Jardetzky,et al. Nuclear magnetic resonance spectroscopy of amino acids, peptides, and proteins. , 1970, Advances in protein chemistry.
[3] H. Scheraga,et al. Experimental and theoretical aspects of protein folding. , 1975, Advances in protein chemistry.