Hydrodynamic properties of nitrogenase - The MoFe protein from Azotobacter vinelandii studied by dynamic light scattering and hydrodynamic modelling

Hellweg T, Eimer W, Krahn E, Schneider K, Müller A (1997)
Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology 1337(2): 311-318.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
Download
Es wurden keine Dateien hochgeladen. Nur Publikationsnachweis!
DOI
Autor*in
Hellweg, ThomasUniBi ; Eimer, W; Krahn, E; Schneider, KlausUniBi; Müller, AchimUniBi
Einrichtung
Fakultät für Chemie > Biochemie I
Fakultät für Chemie > Physikalische und Biophysikalische Chemie
Fakultät für Chemie > Anorganische Chemie I
Abstract / Bemerkung
Experimental results for the nitrogenase MoFe protein from Azotobacter vinelandii obtained by dynamic light scattering (DLS) are presented. The translational diffusion coefficient was determined to D = (4.0 +/- 0.2) x 10(-7) cm(2)/s. Complementary, we have performed hydrodynamic model calculations based on the X-ray crystallographic data of the MoFe protein. The calculated transport coefficient suggests that the size and shape of the protein in solution is consistent with that in the crystal structure.
Stichworte
dynamic light scattering; hydrodynamic model calculation; nitrogenase; (A-vinelandii); translational diffusion
Erscheinungsjahr
1997
Zeitschriftentitel
Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
Band
1337
Ausgabe
2
Seite(n)
311-318
ISSN
0167-4838
Page URI
https://pub.uni-bielefeld.de/record/1637990

Zitieren

Hellweg T, Eimer W, Krahn E, Schneider K, Müller A. Hydrodynamic properties of nitrogenase - The MoFe protein from Azotobacter vinelandii studied by dynamic light scattering and hydrodynamic modelling. Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology. 1997;1337(2):311-318.
Hellweg, T., Eimer, W., Krahn, E., Schneider, K., & Müller, A. (1997). Hydrodynamic properties of nitrogenase - The MoFe protein from Azotobacter vinelandii studied by dynamic light scattering and hydrodynamic modelling. Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology, 1337(2), 311-318. https://doi.org/10.1016/S0167-4838(96)00179-3
Hellweg, Thomas, Eimer, W, Krahn, E, Schneider, Klaus, and Müller, Achim. 1997. “Hydrodynamic properties of nitrogenase - The MoFe protein from Azotobacter vinelandii studied by dynamic light scattering and hydrodynamic modelling”. Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology 1337 (2): 311-318.
Hellweg, T., Eimer, W., Krahn, E., Schneider, K., and Müller, A. (1997). Hydrodynamic properties of nitrogenase - The MoFe protein from Azotobacter vinelandii studied by dynamic light scattering and hydrodynamic modelling. Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology 1337, 311-318.
Hellweg, T., et al., 1997. Hydrodynamic properties of nitrogenase - The MoFe protein from Azotobacter vinelandii studied by dynamic light scattering and hydrodynamic modelling. Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology, 1337(2), p 311-318.
T. Hellweg, et al., “Hydrodynamic properties of nitrogenase - The MoFe protein from Azotobacter vinelandii studied by dynamic light scattering and hydrodynamic modelling”, Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology, vol. 1337, 1997, pp. 311-318.
Hellweg, T., Eimer, W., Krahn, E., Schneider, K., Müller, A.: Hydrodynamic properties of nitrogenase - The MoFe protein from Azotobacter vinelandii studied by dynamic light scattering and hydrodynamic modelling. Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology. 1337, 311-318 (1997).
Hellweg, Thomas, Eimer, W, Krahn, E, Schneider, Klaus, and Müller, Achim. “Hydrodynamic properties of nitrogenase - The MoFe protein from Azotobacter vinelandii studied by dynamic light scattering and hydrodynamic modelling”. Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology 1337.2 (1997): 311-318.

10 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

Label-Free Measurements of Tenofovir Diffusion Coefficients in a Microbicide Gel Using Raman Spectroscopy.
Chuchuen O, Maher JR, Simons MG, Peters JJ, Wax AP, Katz DF., J Pharm Sci 106(2), 2017
PMID: 27837968
Mutations in hpyAVIBM, C⁵ cytosine DNA methyltransferase from Helicobacter pylori result in relaxed specificity.
Kumar R, Sabareesh V, Mukhopadhyay AK, Rao DN., FEBS J 279(6), 2012
PMID: 22269034
Hydrodynamic effects in proteins.
Szymczak P, Cieplak M., J Phys Condens Matter 23(3), 2011
PMID: 21406855
The DFPase from Loligo vulgaris in sugar surfactant-based bicontinuous microemulsions: structure, dynamics, and enzyme activity.
Wellert S, Tiersch B, Koetz J, Richardt A, Lapp A, Holderer O, Gäb J, Blum MM, Schulreich C, Stehle R, Hellweg T., Eur Biophys J 40(6), 2011
PMID: 21416312
Prediction of hydrodynamic and other solution properties of rigid proteins from atomic- and residue-level models.
Ortega A, Amorós D, García de la Torre J., Biophys J 101(4), 2011
PMID: 21843480
Clathrin triskelia show evidence of molecular flexibility.
Ferguson ML, Prasad K, Boukari H, Sackett DL, Krueger S, Lafer EM, Nossal R., Biophys J 95(4), 2008
PMID: 18502808
Proteins in a shear flow.
Szymczak P, Cieplak M., J Chem Phys 127(15), 2007
PMID: 17949222
Precise boundary element computation of protein transport properties: Diffusion tensors, specific volume, and hydration.
Aragon S, Hahn DK., Biophys J 91(5), 2006
PMID: 16714342
Numerical path integration technique for the calculation of transport properties of proteins.
Kang EH, Mansfield ML, Douglas JF., Phys Rev E Stat Nonlin Soft Matter Phys 69(3 pt 1), 2004
PMID: 15089333
Calculation of hydrodynamic properties of globular proteins from their atomic-level structure.
García De La Torre J, Huertas ML, Carrasco B., Biophys J 78(2), 2000
PMID: 10653785

References

Daten bereitgestellt von Europe PubMed Central.

Export

Markieren/ Markierung löschen
Markierte Publikationen

Open Data PUB

Web of Science

Dieser Datensatz im Web of Science®
Quellen

PMID: 9048909
PubMed | Europe PMC

Suchen in

Google Scholar