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Deviations from experimental distance constraints

Table V Deviations from Experimental Distance Constraints for Various Structural Solutions for Globoside... Table V Deviations from Experimental Distance Constraints for Various Structural Solutions for Globoside...
The good agreement between the folded and the experimental structure is also evident from Figure (l)(center), which shows the secondary structure alignment of the native and the folded conformations. The good physical alignment of the helices illustrates the importance of hydrophobic contacts to correctly fold this protein. An independent measure to assess the quality of these contacts is to compare the C -C distances (which correspond to the NOE constraints of the NMR experiments that determine tertiary structure) in the folded structure to those of the native structure. We found that 66 % (80 %) of the C/3-C/3 distance distances agree to within one (1.5) standard deviations of the experimental resolution. [Pg.565]


See other pages where Deviations from experimental distance constraints is mentioned: [Pg.250]    [Pg.259]    [Pg.16]    [Pg.341]    [Pg.1093]    [Pg.1874]    [Pg.53]    [Pg.242]    [Pg.45]    [Pg.150]    [Pg.472]    [Pg.118]   
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Deviations from experimental distance

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