Zobrazeno 1 - 10
of 54
pro vyhledávání: '"Fritz Parak"'
Autor:
Fritz Parak, Hans Frauenfelder
Publikováno v:
Physica A: Statistical Mechanics and its Applications. 201:332-345
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7822e88fd71a5bb797fc6564aa3a29b8
https://doi.org/10.1016/0378-4371(93)90431-3
https://doi.org/10.1016/0378-4371(93)90431-3
Protein motions are essential for function. Comparing protein processes with the dielectric fluctuations of the surrounding solvent shows that they fall into two classes: nonslaved and slaved. Nonslaved processes are independent of the solvent motion
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::25f47892af0adc527417c620cb32c46a
https://europepmc.org/articles/PMC138562/
https://europepmc.org/articles/PMC138562/
Publikováno v:
Physical Chemistry Chemical Physics (PCCP); Sep2005, Vol. 7 Issue 19, p3472-3477, 6p
Autor:
Enrico Clementi, Fritz Parak
Publikováno v:
International Journal of Quantum Chemistry. 59:261-262
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5e26d157c558c0aa536c3fb4cb701436
https://doi.org/10.1002/qua.560590402
https://doi.org/10.1002/qua.560590402
Publikováno v:
Annual Review of Biophysics and Biophysical Chemistry. 17:451-479
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::477238eb699f84b8f20218f4f559eab1
https://doi.org/10.1146/annurev.bb.17.060188.002315
https://doi.org/10.1146/annurev.bb.17.060188.002315
Publikováno v:
Hoppe-Seyler´s Zeitschrift für physiologische Chemie. 359:857-862
M. luteus catalase dissociates upon treatment with urea, dodecylsulfate and anhydrides into monomers, the molecular weight of which appears to be 1/4 of that of the native enzyme. The urea-induced dissociation depends upon the incubation time, the ur
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::df7aba1e8c572d4acdd5c8616ef6e5ff
https://doi.org/10.1515/bchm2.1978.359.2.857
https://doi.org/10.1515/bchm2.1978.359.2.857
Publikováno v:
Zeitschrift für Naturforschung B. 29:241-244
Single crystals of myoglobin enriched on Fe57 with a diameter of about 0.5 mm were prepared. After deoxygenation crystallographic alignment and Mössbauer measurements were carried out at 77°K. In the experiment eight different orientations were sel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::034e9c607d633869fd5e4b1e15f80b50
https://doi.org/10.1515/znb-1974-3-424
https://doi.org/10.1515/znb-1974-3-424
Autor:
Hermann Hartmann, D R Ponzi, Hans Frauenfelder, W. Steigemann, Fritz Parak, Gregory A. Petsko
Publikováno v:
Proceedings of the National Academy of Sciences. 79:4967-4971
The crystal structure of sperm whale metmyoglobin has been determined at 80 K to a resolution of 2A. The overall structure at 80 K is similar to that at 300 K except that the volume is smaller. Refinement of the structure by the method of restrained
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1fbb741e7fa876d6f36998e34e5ec416
https://doi.org/10.1073/pnas.79.16.4967
https://doi.org/10.1073/pnas.79.16.4967
Autor:
Fritz Parak
Publikováno v:
The Enzyme Catalysis Process ISBN: 9781475716092
This contribution shows how X-ray structure analysis and Mossbauer spectroscopy can be used as complementary methods in the investigation of protein dynamics. X-ray analysis measures structural distributions via mean square displacements without havi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::dec463dcd197f0a5425ea65ada195b9f
https://doi.org/10.1007/978-1-4757-1607-8_14
https://doi.org/10.1007/978-1-4757-1607-8_14
Autor:
Fritz Parak
Publisher Summary This chapter summarizes the results on the correlation of the internal mobility of biomolecules with the mobility of the surrounding water as determined by Mossbauer absorption spectroscopy and the Rayleigh scattering of Mossbauer r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::57f905b2be552039c76da8c2ff0cdb45
https://doi.org/10.1016/0076-6879(86)27016-0
https://doi.org/10.1016/0076-6879(86)27016-0