Publication

Anisotropic Local Motions and Location of Amide Protons in Proteins

Geoffrey Bodenhausen
2005
Journal Articles

Résumé

A new method has been developed to obtain dynamic and structural information about peptide planes in proteins by a combination of measurements of weak short-range cross-correlation rates R(HNN/NC') that are due to concerted fluctuations of the HN-N and N-C' dipole-dipole interactions and stronger long-range cross-correlation rates R(C'HN/HNN) and R(NHN/HNCa). The rates were interpreted using the axially sym. Gaussian axial fluctuation model (GAF). The oscillation amplitudes as well as the positions of HN atoms with respect to peptide planes in ubiquitin were detd. Most N-HN bonds were found not to lie exactly along the bisector of the N-C' and N-Ca bonds but to be slightly tilted toward the carbon-terminal side of the peptide. [on SciFinder (R)]

Source officielle

https://infoscience.epfl.ch/entities/publication/d356ce95-8fb4-46bf-b7f0-5a38a8899111

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Geoffrey Bodenhausen
2005
Journal Articles

Résumé

Source officielle

https://infoscience.epfl.ch/entities/publication/d356ce95-8fb4-46bf-b7f0-5a38a8899111

À propos de ce résultat

Concepts associés (19)

Bioinformatique structurale

vignette|262x262px| Structure tridimensionnelle d'une protéine La bioinformatique structurale est la branche de la bio-informatique liée à l'analyse et à la prédiction de la structure tridimensionnelle des macromolécules biologiques telles que les protéines, l'ARN et l'ADN. Elle traite des généralisations sur les structures tridimensionnelles des macromolécules, telles que les comparaisons des repliements globaux et des motifs locaux, les principes du repliement moléculaire, l'évolution, les interactions de liaison et les relations structure/fonction, en travaillant à la fois à partir de structures résolues expérimentalement et de modèles informatiques.

Structural alignment

Structural alignment attempts to establish homology between two or more polymer structures based on their shape and three-dimensional conformation. This process is usually applied to protein tertiary structures but can also be used for large RNA molecules. In contrast to simple structural superposition, where at least some equivalent residues of the two structures are known, structural alignment requires no a priori knowledge of equivalent positions.

Structural genomics

Structural genomics seeks to describe the 3-dimensional structure of every protein encoded by a given genome. This genome-based approach allows for a high-throughput method of structure determination by a combination of experimental and modeling approaches. The principal difference between structural genomics and traditional structural prediction is that structural genomics attempts to determine the structure of every protein encoded by the genome, rather than focusing on one particular protein.

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