Processing of heteronuclear NMR relaxation data with the new software DASHA

The new program DASHA is an efficient implementation of common data processing steps for the protein internal dynamic analysis. The "model-free" parameters and their uncertainties (Lipari G., Szabo A.: J. Am. Chem. Soc. 104, 4546-4559 (1982) can be calculated from an arbitrary combination of experimental data sets (i.e. heteronuclear1H-15N or1H-13C relaxation times and NOE values at different spectrometer frequencies). Anisotropy of the molecular rotational diffusion could be also taken into account without introduction of the new adjustable parameters into the spectral density function J(ω), provided the structure of the molecule is known. Parameters of chemical (conformational) exchange can be estimated from the CPMG spin-lock frequency dependences (Bloom et al.: J. Chem. Phys. 42, 1615-1624 (1965); Orekhov et al.: Eur. J. Biochem. 219, 887-896 (1994). The program can be used both in the interactive and batch modes. It has sophisticated PostScript plotting facilities. © 1995 Springer.