## Abstract NMR–chemical shift structure correlations were investigated by using GIAO‐RB3LYP/6‐311++G(2d,2p) formalism. Geometries and chemical shifts (CSI values) of 103 different conformers of N′‐formyl‐L‐histidinamide were determined including both neutral and charged protonation forms. Correlat
✦ LIBER ✦
Evolution of protein 3D structures as diffusion in multidimensional conformational space
✍ Scribed by Alexander M. Gutin; Azat Ya. Badretdinov
- Publisher
- Springer
- Year
- 1994
- Tongue
- English
- Weight
- 340 KB
- Volume
- 39
- Category
- Article
- ISSN
- 0022-2844
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✦ Synopsis
A theory of protein spatial-structure evolution in terms of random walks in multidimensional conformational space is proposed. It is shown that the spatial divergence in pairs of homologous proteins depends only on their sequence similarity and is independent of the protein size. X-ray data are reasonably well described in terms of the theory developed.
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