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Micka?l?Krzeminski Karine?Loth Rolf?Boelens Alexandre?MJJ?BonvinEmail author 《BMC bioinformatics》2010,11(1):51
Background
The activity of proteins within the cell is characterized by their motions, flexibility, interactions or even the particularly intriguing case of partially unfolded states. In the last two cases, a part of the protein is affected either by binding or unfolding and the detection of the respective perturbed and unperturbed region(s) is a fundamental part of the structural characterization of these states. This can be achieved by comparing experimental data of the same protein in two different states (bound/unbound, folded/unfolded). For instance, measurements of chemical shift perturbations (CSPs) from NMR 1H-15N HSQC experiments gives an excellent opportunity to discriminate both moieties. 相似文献2.
Panagiotis L Kastritis Alexandre MJJ Bonvin 《Current opinion in structural biology》2013,23(6):868-877
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