Outline of a Computer Program for the Analysis of Protein NMR Spectra
It was realized early on in the work process preceeding the determination of three-dimensional structures of proteins in solution by 1H NMR spectroscopy that the very large amount of data in the analysis required the use of computers, primarily as computational devices for ‘number-crunching’; however, the potential of the computer as a bookkeeper and an automation device was also anticipated. The result has been the development of a large number of computer programs, that can assist the analysis of protein NMR data at all levels, from Fourier transformation, automated cross peak identification, amino acid spin system recognition, and sequential and stereospecific assignments.1–10 The development in this field has been promising. In particular, recent analyses of three- and four-dimensional spectra have shown that the larger dispersion of these favors automation.10 However, the full automation of the analysis of protein two-dimensional NMR data involving complete assignment of both NOESY, TOCSY and COSY spectra, full integration of peak volumes, and accurate determination of coupling constants has not yet been achieved. The major reason for this is partly the complexity of the problem, partly the coincidental overlap of resonances, and partly the line broadening of nuclei in certain regions of proteins.
KeywordsSpin System Cross Peak Amino Acid Type Sequential Assignment Common Amino Acid
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