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Capitalised all of DASHA.
The software Dasha DASHA is designed for the model-free analysis for NMR relaxation data. Dasha DASHA can be used as an optimisation engine to replace the minimisation algorithms implemented within relax.
== Website ==
The original Dasha DASHA website is http://www.nmr.ru/dasha.html (and [https://web.archive.org/web/20150223190004/http://www.nmr.ru/dasha.html archived on the Internet Archive]).
== Overview ==
From the Dasha DASHA homepage:
{{quote|text=DASHA is an interactive program designed to investigate dynamics of biomolecules, for which data of <sup>15</sup>N or <sup>13</sup>C heteronuclear relaxation are available from NMR measurements. A number of sets of longitudinal and transverse relaxation rates of <sup>15</sup>N or <sup>13</sup>C nuclei and <sup>1</sup>H-<sup>15</sup>N, <sup>13</sup>C NOE's obtained at various NMR spectrometer frequencies might be used as the input. The measured longitudinal, transverse relaxation rates and NOE values are interpreted using the model-free approach of Lipari and Szabo (1982, J. Am. Chem. Soc., 104, 4546-4559). In addition to the overall rotational correlation time of the molecule, the internal dynamics of backbone N-H or C-H vectors of two types of internal motions - fast, on a time scale of <20 ps, and intermediate, close to 1 ns could be evaluated by constructing correspondent spectral density functions. Contribution of the conformational exchange to transverse relaxation rates of individual nitrogens or carbons could be elucidated using a set of different rates of the CPMG spin-lock pulse train in measuring {{:T2}} relaxation times (Orekhov et al., 1994, Eur. J. Biochem., 219, 887-896). Separate module DIFFC, included into the DASHA software, performs hydrodynamic calculations for proteins with known spatial structure. All input and output data could be easily presented in PostScript format.}}
