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Conformational derivatives

Fig. 2.31 Comparison of the turn segment found in hairpin 122 with a naturally-occuring type II / -turn of a-polypeptides together with backbone dihedral angles in degrees. In the case of 122, the angles were extracted from one low energy conformer derived from NMR data and shown in Fig. 2.30. Torsion angles with comparable values are shown in bold [191, 195]... Fig. 2.31 Comparison of the turn segment found in hairpin 122 with a naturally-occuring type II / -turn of a-polypeptides together with backbone dihedral angles in degrees. In the case of 122, the angles were extracted from one low energy conformer derived from NMR data and shown in Fig. 2.30. Torsion angles with comparable values are shown in bold [191, 195]...
Gresh N, Claverie P, Pullman A (1984) Theoretical studies of molecular conformation. Derivation of an additive procedure for the computation of intramolecular interaction energies. Comparison with ab initio SCF computations. Theor Chim 66(l) l-20... [Pg.169]

N. Gresh, P. Glaverie, and A. Pullman, Theor. Chim. Acta, 66,1 (1984). Theoretical Studies of Molecular Conformation. Derivation of an Additive Procedure for the Computation of Intramolecular Interaction Energies Comparison with Ab Initio SCF Computations. [Pg.287]

Fig. 13 The distance distribution for ASYN bound to LUV and labeled at residue 27 and 56 clearly consists of two contributions. The shorter distance agrees well with the expected distance of 2.7 nm for the horseshoe conformation derived from the NMR structure (pdb access code 1XQ8) while the longer distance is consistent with an extended alpha-helix. Taken from [140]... Fig. 13 The distance distribution for ASYN bound to LUV and labeled at residue 27 and 56 clearly consists of two contributions. The shorter distance agrees well with the expected distance of 2.7 nm for the horseshoe conformation derived from the NMR structure (pdb access code 1XQ8) while the longer distance is consistent with an extended alpha-helix. Taken from [140]...
Figure 8.58. Helical structures of 10 overlaid low-energy conformers derived for the hexameric /3-peptide 8.25 shown as side-on (left) and top-down (right) views. The -butyldimethylsilyl (TBDMS) protecting groups are not shown beyond the silicon atom. These figures appear in colour on the back cover. Figure 8.58. Helical structures of 10 overlaid low-energy conformers derived for the hexameric /3-peptide 8.25 shown as side-on (left) and top-down (right) views. The -butyldimethylsilyl (TBDMS) protecting groups are not shown beyond the silicon atom. These figures appear in colour on the back cover.

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See also in sourсe #XX -- [ Pg.147 ]




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