期刊
JOURNAL OF MAGNETIC RESONANCE
卷 160, 期 1, 页码 33-39出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/S1090-7807(02)00138-6
关键词
solid-state NMR; PISEMA; torsion angles; angular constraints; protein structure; PISA wheel
资金
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R37GM024266, R01GM029754, P01GM056538] Funding Source: NIH RePORTER
- NIGMS NIH HHS [R01GM29754, P01GM 56538, R37GM24266] Funding Source: Medline
An algorithm for fitting protein structures to PISEMA spectra is described, and its application to helical proteins in aligned samples is demonstrated using both simulated and experimental results. The formulation of the algorithm in terms of rotation operators yields compact recursion relations that provide a fast and effective way of obtaining peptide plane orientations from chemical and torsion angle constraints. The algorithm in combination with experimental solid-state NMR data results in a method for determining the backbone structures of proteins, since it yields the orientation of a helix as a whole, including its tilt and twist angles, and describes kinks and curves with atomic resolution. Although the algorithm can be applied in an assignment-free manner to spectra of uniformly labeled proteins, the precision of the structural fitting is improved by the addition of assignment information, for example the identification of resonances by residue type from spectra of selectively labeled proteins. (C) 2002 Elsevier Science (USA). All rights reserved.
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