Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Ines M. Li De La Sierra"'
Autor:
and Octavian Bârzu, ‡ Anne-Marie Gilles, Ines M. Li De La Sierra, Michel Vincent, Pierre Briozzo, Jacques Gallay
Publikováno v:
The Journal of Physical Chemistry B. 104:11286-11295
The fluorescent dynamic Stokes shift (FDSS) method has emphasized a time-dependent dipolar relaxation process around the single tryptophan residue (Trp31) in cytidine monophosphate kinase from E. coli (CMPK). This Trp residue, located close to the pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2909d2c1153f8c9fbe9f19ba8282fbb6
https://doi.org/10.1021/jp000638x
https://doi.org/10.1021/jp000638x
Autor:
Ines M. Li de la Sierra, Gabriel Padrón, Juan Madrazo, Julio G. Alvarez, Raimundo Ubieta, Michel Vincent, Jacques Gallay
Publikováno v:
European journal of biochemistry. 211(1-2)
A time-resolved fluorescence spectroscopic study of the recombinant human epidermal growth factor (hEGF), a bis(tryptophan)-containing protein (Trp49-Trp50), and of the two single-tryptophan-containing engineered mutants with Trp49 or Trp50 replaced
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8180e6d80341f2db1e7179ca663b0e45
https://pubmed.ncbi.nlm.nih.gov/8425531
https://pubmed.ncbi.nlm.nih.gov/8425531
Autor:
Michel Vincent, Jacques Gallay, Ines M. Li De La Sierra, Gabriel Padrón, Aída Diaz, Mário N. Berberan-Santos, Maylin Diaz
Publikováno v:
European journal of biochemistry. 210(3)
Human recombinant interferon alpha 2 belongs a to family of proteins active against a wide range of viruses. It contains two tryptophan residues located at positions 77 and 141 in the peptide sequence. The fluorescence emission spectrum of these tryp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c3eb36eda8ba46947733b4c910f56b56
https://pubmed.ncbi.nlm.nih.gov/1483478
https://pubmed.ncbi.nlm.nih.gov/1483478
Autor:
Ines M. Li De La Sierra, Thierry Prangé, Alexis Musacchio, Roger Fourme, Pablo Fuentes, Juan Madrazo, Gabriel Padrón
Publikováno v:
Journal of Molecular Biology. 235:1154-1155
A protein constituent of the outer membrane from Neisseria meningitidis (hereafter called P64K) has been crystallized using the hanging drop technique. Crystals are tetragonal with unit cell dimensions a = b = 136·84 A and c = 78·44 A, compatible w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::31b764cffe056e8df33fb8ce0712649d
https://doi.org/10.1006/jmbi.1994.1067
https://doi.org/10.1006/jmbi.1994.1067