Hasil untuk "physics.comp-ph"

R. Martínez‐Zaguilán, E. Seftor, R. E. Seftor et al.

M. Lemmon, K. Ferguson, J. Schlessinger

With the identification of two distinct classes of high affinity, physiologically relevant, ligands for PH domains, it appears reasonable to assume that additional specific high affinity ligands for other PH domains will be identified in the future. It is not clear, however, whether each of the 90 proposed PH domains will have its own specific ligand. Possible candidates for specific PH domain ligands include various inositol polyphosphates, phosphorylated membrane components, as well as specific protein sequences containing phosphorylated tyrosine, serine, threonine, or histidine residues. It appears unlikely that the low affinity interactions of phosphoinositides described for several PH domains are physiologically relevant. It is difficult to imagine why such a large and diverse family of PH domains (with just 10-15% sequence identity) would exist in order to bind with a similar low affinity to PtdInsP2-containing membranes. Rather, we suggest that these interactions represent limited binding to noncognate ligands - the physiologically relevant ligands have yet to be identified. It is likely that many, if not all, PH domains have their own high affinity, cell membrane-associated, ligands and operate according to the paradigms described for the PH domains of PLCδ1 and Shc (Figure 2Figure 2A and Figure 2Figure 2B). The structural homology between PH domains might reflect a particularly stable protein scaffold of β sheets that can present variable ligand-binding loops in a manner analogous to that seen in the immunoglobulin superfamily.

Feng Xu

The electronic absorption spectrum, susceptibility to fluoride inhibition, redox potential, and substrate turnover of several fungal laccases have been explored as a function of pH. The laccases showed a single spectrally detectable acid-base transition at pH 6-9 and a fluoride inhibition that diminished by increased pH (indicating a competition with hydroxide inhibition). Relatively small changes in the redox potentials (≤0.1 V) of laccase were observed over the pH 2.7-11. Under the catalysis of laccase, the apparent oxidation rates (kcat and kcat/Km) of two nonphenolic substrates, potassium ferrocyanide and 2,2′-azinobis-(3-ethylbenzthiazoline-6-sulfonic acid),decreased monotonically as the pH increased. In contrast, the apparent oxidation rates (kcat and kcat/Km) of three 2,6-dimethoxyphenols (whose pKa values range from 7.0 to 8.7) exhibited bell-shaped pH profiles whose maxima were distinct for each laccase but independent of the substrate. By correlating these pH dependences, it is proposed that the balance of two opposing effects, one generated by the redox potential difference between a reducing substrate and the type 1 copper of laccase (which correlates to the electron transfer rate and is favored for a phenolic substrate by higher pH) and another generated by the binding of a hydroxide anion to the type 2/type 3 coppers of laccase (which inhibits the activity at higher pH), contributes to the pH activity profile of the fungal laccases.

I. J. Buerge, S. Hug

M. Dockal, D. Carter, F. Rüker

Human serum albumin (HSA) is a protein of 66.5 kDa that is composed of three homologous domains, each of which displays specific structural and functional characteristics. HSA is known to undergo different pH-dependent structural transitions, the N-F and F-E transitions in the acid pH region and the N-B transition at slightly alkaline pH. In order to elucidate the structural behavior of the recombinant HSA domains as stand-alone proteins and to investigate the molecular and structural origins of the pH-induced conformational changes of the intact molecule, we have employed fluorescence and circular dichroic methods. Here we provide evidence that the loosening of the HSA structure in the N-F transition takes place primarily in HSA-DOM III and that HSA-DOM I undergoes a structural rearrangement with only minor changes in secondary structure, whereas HSA-DOM II transforms to a molten globule-like state as the pH is reduced. In the pH region of the N-B transition of HSA, HSA-DOM I and HSA-DOM II experience a tertiary structural isomerization, whereas with HSA-DOM III no alterations in tertiary structure are observed, as judged from near-UV CD and fluorescence measurements.

D. Sifrim, R. Holloway, J. Silny et al.

J. Kellum

An advanced understanding of acid–base physiology is as central to the practice of critical care medicine, as are an understanding of cardiac and pulmonary physiology. Intensivists spend much of their time managing problems related to fluids, electrolytes, and blood pH. Recent advances in the understanding of acid–base physiology have occurred as the result of the application of basic physical-chemical principles of aqueous solutions to blood plasma. This analysis has revealed three independent variables that regulate pH in blood plasma. These variables are carbon dioxide, relative electrolyte concentrations, and total weak acid concentrations. All changes in blood pH, in health and in disease, occur through changes in these three variables. Clinical implications for these findings are also discussed.

J. Horiuchi, T. Shimizu, K. Tada et al.

S. Maberly

K. Loftin, C. Adams, M. Meyer et al.

Cecilia Sundberg, S. Smårs, Håkan Jönsson

P. J. Hansen

C. Hsiao, C. Chiou, J. Yang

M. Cohen, Xi-ming Yang, J. Downey

B. Singh, B. Singh, A. Walker et al.

F. Zerbib, S. B. Varannes, S. Roman et al.

Autumn S. Wang, J. Angle, R. Chaney et al.

S. Bishnoi, C. Rozell, C. Levin et al.

N. Maalouf, M. Cameron, O. Moe et al.

A. Burbano, D. Dionysiou, M. Suidan et al.