Related Articles1H NMR study of dynamics and thermodynamics of acid-alkaline transition in ferric hemoglobin of a midge larva (Tokunagayusurika akamusi).
Biochim Biophys Acta. 1998 Jun 11;1385(1):89-100
Authors: Koshikawa K, Yamamoto Y, Kamimura S, Matsuoka A, Shikama K
One of the components of hemoglobin from the larval hemolyph of Tokunagayusurika akamusi possesses naturally occurring substitution at the E7 helical position (Leu E7) [M. Fukuda, T. Takagi, K. Shikama, Biochim. Biophys. Acta 1157 (1993) 185-191]. Its oxygen affinity is almost comparable to those of mammalian myoglobins and it exhibits Bohr effect. Both acidic and alkaline forms of the ferric hemoglobin have been investigated using 1H NMR in order to gain insight into molecular mechanisms for relatively high oxygen affinity and Bohr effect of this protein. The NMR data indicated that the acidic form of the protein possesses pentacoordinated heme, and that the alkaline form possessing OH- appears with increasing the pH value. pH titration yielded a pK value of 7.2 for the acid-alkaline transition, and this value is the lowest among the values reported so far for various myoglobins and hemoglobins. The kinetic measurements of the transition revealed that the activation energy for the dissociation of the Fe-bound OH-, as well as the dissociation and association rates, decrease with increasing the pH value. These pH dependence properties are likely to be related to the Bohr effect of this protein.
Solution structure, dynamics and thermodynamics of the three SH3 domains of CD2AP
Solution structure, dynamics and thermodynamics of the three SH3 domains of CD2AP
Abstract CD2 associated protein (CD2AP) is an adaptor protein that plays an important role in cell to cell union needed for the kidney function. It contains three N-terminal SH3 domains that are able to interact among others with CD2, ALIX, c-Cbl and Ubiquitin. To understand the role of the individual SH3 domains of this adaptor protein we have performed a complete structural, thermodynamic and dynamic characterization of the separate domains using NMR and DSC. The energetic contributions to the stability...
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05-01-2011 04:48 AM
[NMR paper] NMR investigation of the alkaline-like conformational transition of horse heart cytoc
NMR investigation of the alkaline-like conformational transition of horse heart cytochrome c in the presence of exogenous thiazole.
Related Articles NMR investigation of the alkaline-like conformational transition of horse heart cytochrome c in the presence of exogenous thiazole.
Biophys Chem. 2003 Jun 1;104(2):459-68
Authors: Yao Y, Tang W
The conformational transition of horse heart cyt c in the presence of exogenous thiazole is investigated by NMR spectroscopy. Surprisingly, besides the native form and the ligand-bound form, another species...
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11-24-2010 09:01 PM
[NMR paper] NMR study of the binding of all-trans-retinoic acid to type II human cellular retinoi
NMR study of the binding of all-trans-retinoic acid to type II human cellular retinoic acid binding protein.
Related Articles NMR study of the binding of all-trans-retinoic acid to type II human cellular retinoic acid binding protein.
Biochim Biophys Acta. 1999 Aug 17;1433(1-2):240-52
Authors: Wang L, Yan H
Cellular RA binding proteins are thought to play important roles in the (RA), a hormonally active metabolite of vitamin A that has profound effects on cell growth, + differentiation and morphogenesis. Binding of RA to type II human cellular...
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11-18-2010 08:31 PM
NMR study of hydrogen exchange during the B-Z transition of a DNA duplex induced by t
NMR study of hydrogen exchange during the B-Z transition of a DNA duplex induced by the Z? domains of yatapoxvirus E3L.
Related Articles NMR study of hydrogen exchange during the B-Z transition of a DNA duplex induced by the Z? domains of yatapoxvirus E3L.
FEBS Lett. 2010 Oct 8;
Authors: Lee EH, Seo YJ, Ahn HC, Kang YM, Kim HE, Lee YM, Choi BS, Lee JH
The Yaba-like disease viruses (YLDV) are members of the Yatapoxvirus family and have double-stranded DNA genomes. The E3L protein, which is essential for pathogenesis in the vaccinia virus,...
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10-13-2010 02:18 PM
[NMR thesis] Nuclear spin dynamics and thermodynamics of pulsed NMR in solids
Nuclear spin dynamics and thermodynamics of pulsed NMR in solids
Burum, Douglas Peter (1979) Nuclear spin dynamics and thermodynamics of pulsed NMR in solids. Dissertation (Ph.D.), California Institute of Technology. http://resolver.caltech.edu/CaltechETD:etd-04302007-153624
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08-27-2010 01:45 AM
[NMR paper] Thermodynamics of unfolding of ribonuclease A under high pressure. A study by proton
Thermodynamics of unfolding of ribonuclease A under high pressure. A study by proton NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Thermodynamics of unfolding of ribonuclease A under high pressure. A study by proton NMR.
J Mol Biol. 1995 Jul 28;250(5):689-94
Authors: Yamaguchi T, Yamada H, Akasaka K
Thermodynamic stability of ribonuclease A (6.2 mM pH 1.0, 0.15 M KCl, in 2H2O) has been studied in the pressure range of 1 to 2000 atm and in the temperature range...
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08-22-2010 03:50 AM
[NMR paper] Structure and dynamics of the acid-denatured molten globule state of alpha-lactalbumi
Structure and dynamics of the acid-denatured molten globule state of alpha-lactalbumin: a two-dimensional NMR study.
Related Articles Structure and dynamics of the acid-denatured molten globule state of alpha-lactalbumin: a two-dimensional NMR study.
Biochemistry. 1993 Feb 23;32(7):1707-18
Authors: Alexandrescu AT, Evans PA, Pitkeathly M, Baum J, Dobson CM
Two-dimensional 1H-NMR spectroscopy has been used to study the acid-denatured molten globule (A-state) of alpha-lactalbumin. The NMR spectra show that chemical shift dispersion is limited...
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08-21-2010 11:53 PM
[NMR paper] NMR studies of protein-nucleic acid complexes: structures, solvation, dynamics and co
NMR studies of protein-nucleic acid complexes: structures, solvation, dynamics and coupled protein folding.
Related Articles NMR studies of protein-nucleic acid complexes: structures, solvation, dynamics and coupled protein folding.
Q Rev Biophys. 1999 Feb;32(1):57-98
Authors: Härd T