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Thermal denaturation of rSBA and gSBA Thermal unfolding profiles of both nonglycosylated and glycosylated SBA were monitored by the change in molar ellipticity value at 218 nm at a protein concentration of 13 µM
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Interestingly, although the average shape is independent of sequence in the EV limit, it clearly depends on sequence for folded proteins
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Steady-state and quenching experiments were acquired at 298 K
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2 C and 3 A) (Table 3)
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Principles of Fluorescence Spectroscopy, 2nd ed
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Am J Respir Cell Mol Biol 2006; 34:274-285(44) Botto M, Dell'Agnola C, Bygrave AE, et al
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To derive thermodynamic parameter from spectroscopic data it is crucial whether the signal changes during the unfolding process are proportional to the molar fractions of the folded and unfolded protein
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In the large oocytes of the frog Xenopus laevis, this was small enough to allow the recording of the first compartment-selective in vivo MR spectra from the animal and vegetal cytoplasm as well as the nucleus
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Although glycosylation does not affect the structure, protein dynamic fluctuations decrease globally, decreasing amide hydrogen exchange rates by up to sixfold throughout the entire protein
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The exchange data for all residues are summarized in Fig
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of Physical Chemistry-Laboratory of Biophysical Chemistry, University of Nijmegen, Toernooiveld 1, 6525 ED, Nijmegen, The Netherlands
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Aliquots of the aggregation reaction was withdrawn and assayed to avoid adverse effects of probe binding during the reaction
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Therefore, the following studies were conducted assuming that properties of the membrane surface are largely unchanged in the 1-2000 bar range
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Resolution of a signal transfer region from a general binding domain in Gβ for stimulation of phospholipase C-β2
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The book is divided into ten parts with each part divided into clearly demarcated sub-sections allowing ready reference
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