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The PTS involves a cascade of phosphoryl-transfer steps from phosphoenolpyruvate (PEP) via phosphointermediates of the general cytosolic non-sugar-specific phosphotransferases enzyme I (EI) and the histidine-phosphocarrier (HPr) to sugar-specific enzyme II permeases
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, folded, unfolded), the use of this signal to measure protein stability often gives rise to difficulties
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Protein dynamics from NMR
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These include activation or inhibition of plasma enzymes that are essential in reverse cholesterol transport (Forte et al
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Apolipoprotein A-II, a protein in search of a function
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Exp Cell Res 1992:200:379-92
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Almqvist KF, Wang L, Wang J, et al
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- Centralizing the management of these functions has given us control over many of the variables that might have been left off the table in another day
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. Investigation of the properties of these partially folded states using probes such as ANS or bis-ANS (which bind to exposed hydrophobic domains in proteins) was not possible due to the significant overlap between the emission spectra of these probes when bound to proteins and the excitation spectrum of the prosthetic group, FAD (data not shown)
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. Protein glycosylation is more profuse and structurally more complex than all other types of posttranslational modifications taken together (1-3)
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. In the case of multitryptophan proteins, tyrosine fluorescence emission is generally not visible, mainly due to much larger absorption coefficients and quantum yields of the tryptophans, and at least for folded states because of distinct Förster energy transfer from tyrosines to tryptophans (3,14)
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. ORIGIN software was used for the data analysis and display (OriginLab, Northampton, MA)
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. The Θ^sub 222^(t) data recorded in the second and consecutive jumps were similar, indicating faster unfolding than in the first jump (Fig
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. These may or may not be identified as intermediate states, depending on their occupancy lifetime
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.We followed here a similar procedure to estimate errors on the conformational entropy changes upon complex formation for the sets of atoms that are involved in intermolecular interactions and/or show conformational changes (Table 1)
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