PubMed · 10710777
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G Marshall. 2000. Ancient atomists.. https://pubmed.ncbi.nlm.nih.gov/10710777/
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Structural biologists of all shapes and sizes gathered recently in Breckenridge, Colorado to discuss recent developments in the field. If we are to believe what they said, the future of structural biology is very bright.
One of the key qualities of mass spectrometric measurements for biomolecules is the mass measurement accuracy (MMA) obtained. FTICR presently provides the highest MMA over a broad m/z range. However, due to space charge effects, the achievable MMA crucially depends on the number of ions trapped in the ICR cell for a measurement. Thus, beyond some point, as the effective sensitivity and dynamic range of a measurement increase, MMA tends to decrease. While analyzing deviations from the commonly used calibration law in FTICR we have found systematic errors which are not accounted for by a "global" space charge correction approach. The analysis of these errors and their dependence on charge population and post-excite radius have led us to conclude that each ion cloud experiences a different interaction with other ion clouds. We propose a novel calibration function which is shown to provide an improvement in MMA for all the spectra studied.
We report the initial structure-activity relationship study (SAR) (in particular logP) of a series of compounds based upon 4-sulfamated phenyl ketones as potent inhibitors of the enzyme estrone sulfatase (ES). The results of the study show that these compounds are irreversible inhibitors of ES and that they are more potent than COUMATE, but weaker than EMATE. Analysis of the SAR data shows a strong correlation between IC(50) and logP but also supports our previous study, which suggests a very strong relationship between pK(a) and IC(50).