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Current research on micromechanical resonators strives for quantum-limited detection of the motion of macroscopic objects. Prerequisite to this goal is the observation of measurement backaction consistent with quantum metrology limits. However, thermal noise currently dominates measurements and precludes ground-state preparation of the resonator. Here, we establish the collective motion of an ultracold atomic gas confined tightly within a Fabry–Perot optical cavity as a system for investigating the quantum mechanics of macroscopic bodies. The cavity-mode structure selects a particular collective vibrational motion that is measured by the cavity’s optical properties, actuated by the cavity optical field and subject to backaction by the quantum force fluctuations of this field. Experimentally, we quantify such fluctuations by measuring the cavity-light-induced heating of the intracavity atomic ensemble. These measurements represent the first observation of backaction on a macroscopic mechanical resonator at the standard quantum limit. [ABSTRACT FROM AUTHOR]

Tyrosine O-sulfation is a key post-translational modification that regulates protein-protein interactions in extracellular space. We describe a subtractive strategy to determine the sites of tyrosine O-sulfation in proteins. Hydroxyl groups on unsulfated tyrosines are blocked by stoichiometric acetylation in a one-step reaction using sulfosuccinimidyl acetate (S-NHSAc) in the presence of imidazole at pH 7.0. The presence of sulfotyrosine is indicated by the detection of free tyrosine after tandem mass spectrometry (MS/MS) analysis under conditions in which the sulfuryl group of sulfotyrosine is labile. Since phosphorylation and sulfation of tyrosine are isobaric, we used alkaline phosphatase treatment to distinguish these two modifications. Using this methodology we identified the sites and the order of sulfation of several peptides mediated by purified human tyrosylprotein sulfotransferases (TPSTs), and unambiguously determined the tyrosine sulfation sites in mouse lumican and human vitronectin. [ABSTRACT FROM AUTHOR]