Výsledky vyhledávání - "Markus Blümel"

Autor: Frank Löhr, Markus Blümel, Jürgen M. Schmidt, Heinz Rüterjans

Publikováno v: Journal of Biomolecular NMR. 14:1-12

The concept of self-consistent J coupling evaluation exploits redundant structure information inherent in large sets of 3J coupling constants. Application to the protein Desulfovibrio vulgaris flavodoxin demonstrates the simultaneous refinement of to

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::2e0a961807879affc31eef9de7a6fc57
https://doi.org/10.1023/a:1008345303942

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Autor: Markus Blümel, Jürgen M. Schmidt, Frank Löhr, Heinz Rüterjans

Publikováno v: Journal of Biomolecular NMR. 10:107-118

A triple-resonance NMR technique suitable for the determination ofcarbonyl-related couplings in polypeptide systems is introduced. Theapplication of three novel pulse sequences to uniformly13C/15N-enriched proteins yields E.COSY-likemultiplet pattern

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::e77b2d302e4b5445a77f1b65063f6d43
https://doi.org/10.1023/a:1018355327792

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Autor: Markus Blümel, Heinz Rüterjans, Andrea Hrovat, Frank Löhr, Stephen G. Mayhew

Publikováno v: Journal of Biomolecular NMR. 10:53-62

Recombinant Desulfovibrio vulgaris flavodoxin was produced inEscherichia coli. A complete backbone NMR assignment for the two-electronreduced protein revealed significant changes of chemical shift valuescompared to the oxidized protein, in particular

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::03bfe43b2ab993bba2e65606223a4b25
https://doi.org/10.1023/a:1018380509735

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NMR studies of flavoproteins

Autor: G. Fleischmann, Franz Müller, Markus Blümel, Frank Löhr, Stephen G. Mayhew, Martin A. Knauf, F. Lederer, Heinz Rüterjans

Publikováno v: Biochemical Society Transactions. 24:116-121

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e860865111e13b23f8226eeb0d37db76
https://doi.org/10.1042/bst0240116

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Refined NMR solution structures of proteins using homo- and heteronuclear couplings, relaxation time measurements and relaxation matrix analysis

Autor: Jurema Schmidt, Heinz Rüterjans, Markus Blümel, Jan Engelke, Frank Löhr, Normann Spitzner, Stefania Pfeiffer

Publikováno v: Pure and Applied Chemistry. 68:1329-1334

In order to compare high resolution crystal structures of proteins with the corresponding solution structures a detailed analysis of NMR parameters obtained for various proteins was carried out. As many NOE values as possible were transformed into di

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::550019d094309c4247605e6ed033ff78
https://doi.org/10.1351/pac199668061329

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NMR investigation of the solution conformation of oxidized flavodoxin from Desulfovibrio vulgaris. Determination of the tertiary structure and detection of protein-bound water molecules

Autor: Martin A. Knauf, Markus Blümel, Stephen G. Mayhew, Heinz Rüterjans, Frank Löhr

Publikováno v: European journal of biochemistry. 238(2)

Desulfovibrio vulgaris flavodoxin has been investigated with a combination of homo- and hetero-nuclear two-dimensional and three-dimensional NMR spectroscopy. The analysis of NOE, hydrogen exchange and J-coupling data led to a set of 1349 NOE, 63 hyd

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::770d91823f922285bacc79e9e33795e6
https://pubmed.ncbi.nlm.nih.gov/8681954

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