Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Dietmar Leitner"'
Publikováno v:
Journal of Biomolecular NMR. 31:115-128
The determination of the three-dimensional structure of a protein or the study of protein-ligand interactions requires the assignment of all relevant nuclei as an initial step. This is nowadays almost exclusively performed using triple-resonance expe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff0b631a785b1ec63e1160ae5048f9bc
https://doi.org/10.1007/s10858-004-8263-z
https://doi.org/10.1007/s10858-004-8263-z
Autor:
Urs Wiedemann, Prisca Boisguerin, Gerd Krause, Dietmar Leitner, Rainer Leben, Karin Moelling, Rudolf Volkmer-Engert, Hartmut Oschkinat
Publikováno v:
Journal of Molecular Biology. 343:703-718
Transient macromolecular complexes are often formed by protein-protein interaction domains (e.g. PDZ, SH2, SH3, WW) which recognize linear sequence motifs with in vitro affinities typically in the micromolar range. The analysis of the resulting inter
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::238d88ad87125580017347bc3fdf111a
https://doi.org/10.1016/j.jmb.2004.08.064
https://doi.org/10.1016/j.jmb.2004.08.064
Publikováno v:
Journal of Biomolecular NMR. 25:41-53
The algorithm PLATON is able to assign sets of chemical shifts derived from a single residue to amino acid types with its secondary structure (amino acid species). A subsequent ranking procedure using optionally two different penalty functions yields
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d9b25f70bfc7857c52bfa02bca2829c6
https://doi.org/10.1023/a:1021952400388
https://doi.org/10.1023/a:1021952400388
Autor:
Klaus Weisz, Dietmar Leitner
Publikováno v:
Journal of Biomolecular Structure and Dynamics. 17:993-1000
A set of 21 oligodeoxynucleotides were designed to fold into intramolecular triple helices of the pyrimidine motif under appropriate conditions. UV melting experiments on the triplexes which only differ in the number and distribution of third strand
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9e14aaf37543216feb1272815ee75a84
https://doi.org/10.1080/07391102.2000.10506587
https://doi.org/10.1080/07391102.2000.10506587
Publikováno v:
Biochemistry. 39:5886-5892
To investigate cytosine protonation and its influence on the sequence-dependent thermal stability of DNA triplexes in detail, we have employed homo- and heteronuclear NMR experiments on specifically (15)N-labeled oligodeoxynucleotides that were desig
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e842829a95be8bd31da0afbe4abc2d52
https://doi.org/10.1021/bi992630n
https://doi.org/10.1021/bi992630n
Autor:
Dietmar Leitner, Peter Schmieder, Anne Diehl, Dirk Labudde, Martin Wahl, José R. Pires, Michele Fossi, Martina Leidert, Urs Wiedemann, Gerd Krause, Hartmut Oschkinat
Publikováno v:
FEBS letters. 579(17)
Phox and Bem1 (PB1) domains mediate protein-pro- tein interactions via the formation of homo- or hetero-dimers. The C-terminal PB1 domain of yeast cell division cycle 24 (CDC24p), a guanine-nucleotide exchange factor involved in cell polarity establi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ae959828a4853025fd5a0da0303bb7af
https://pubmed.ncbi.nlm.nih.gov/15961083
https://pubmed.ncbi.nlm.nih.gov/15961083
Publikováno v:
BMC structural biology, 5: 8
BMC Structural Biology, Vol 5, Iss 1, p 8 (2005)
BMC Structural Biology
BMC Structural Biology, Vol 5, Iss 1, p 8 (2005)
BMC Structural Biology
Background A reliable prediction of the Xaa-Pro peptide bond conformation would be a useful tool for many protein structure calculation methods. We have analyzed the Protein Data Bank and show that the combined use of sequential and structural inform
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::2ae037a026bbfc0853623f6ab89907d9
https://repository.publisso.de/resource/frl:6405147
https://repository.publisso.de/resource/frl:6405147
Autor:
Olaf J. Gaiser, Ronald Kühne, Linda J. Ball, Holger Strauss, Martin Wahl, Dietmar Leitner, Udo Heinemann, Hartmut Oschkinat, Peter Schmieder
Publikováno v:
Biochemistry. 43(51)
BRCA1 is a tumor suppressor protein associated with breast and ovarian cancer. The C-terminal region of BRCA1 consists of two closely spaced BRCT domains which mediate essential biological functions, including regulation of transcription and control
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::93f4b9cca994ed2a78ba4a917a4d34b8
https://pubmed.ncbi.nlm.nih.gov/15609993
https://pubmed.ncbi.nlm.nih.gov/15609993
Autor:
Dietmar Leitner, Dirk Labudde, Jens P. Linge, Michael Nilges, Michele Fossi, Hartmut Oschkinat
Publikováno v:
Journal of biomolecular NMR. 31(1)
Large-scale protein structure determination by NMR via automatic assignment of NOESY spectra requires the adjustment of several parameters for optimal performance. Among those are the chemical shift tolerance windows (delta), which allow for the comp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0108c0ccb92fd7dacab5f09ad9453f7f
https://pubmed.ncbi.nlm.nih.gov/15692736
https://pubmed.ncbi.nlm.nih.gov/15692736
Autor:
Dietmar Leitner, Volker Sievert, Ronald Kühne, Dirk Labudde, Annette Diehl, Christoph Brockmann, Hartmut Oschkinat, Konrad Büssow
Publikováno v:
FEBS letters. 558(1-3)
The solution structure of an N-terminally extended construct of the SODD BAG domain was determined by nuclear magnetic resonance spectroscopy. A homology model of the SODD-BAG/HSP70 complex reveals additional possible interactions that are specific f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c9b20edd226ca2d727c19b4512f61ad2
https://pubmed.ncbi.nlm.nih.gov/14759524
https://pubmed.ncbi.nlm.nih.gov/14759524