Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Dieter Perl"'
Autor:
Maik H. Jacob, Franz X. Schmid, Andre E. Merbach, Georg Holtermann, Andreas Martin, Christophe Saudan, Dieter Perl
Publikováno v:
Journal of Molecular Biology. 318:837-845
The cold-shock protein CspB folds rapidly in a N ⇄ U two-state reaction via a transition state that is about 90% native in its interactions with denaturants and water. This suggested that the energy barrier to unfolding is overcome by processes occ
Autor:
Dieter Perl, Franz X. Schmid
Publikováno v:
ChemBioChem. 3:39-44
Publikováno v:
Biochemistry. 40:15501-15511
Residues Arg3 and Leu66 are crucially important for the enhanced stability of the cold shock protein Bc-Csp from the thermophile Bacillus caldolyticus relative to its homologue Bs-CspB from the mesophile Bacillus subtilis. Arg3, which replaces Glu3 o
Publikováno v:
Journal of Molecular Biology. 313:359-369
The cold shock proteins Bc-Csp from the thermophile Bacillus caldolyticus and Bs-CspB from the mesophile Bacillus subtilis differ significantly in their conformational stability, although the two proteins differ by only 12 out of 67 amino acid residu
Publikováno v:
Nature Structural Biology. 7:380-383
Thermophilic organisms produce proteins of exceptional stability. To understand protein thermostability at the molecular level we studied a pair of cold shock proteins, one of mesophilic and one of thermophilic origin, by systematic mutagenesis. Alth
Publikováno v:
Journal of Molecular Biology. 297:975-988
The bacterial cold shock proteins are small compact beta-barrel proteins without disulfide bonds, cis-proline residues or tightly bound cofactors. Bc-Csp, the cold shock protein from the thermophile Bacillus caldolyticus shows a twofold increase in t
Autor:
Mohamed A. Marahiel, Saufung Ma, Peter L. Graumann, Thomas Schindler, Franz X. Schmid, Dieter Perl
Publikováno v:
Journal of Biological Chemistry. 274:3407-3413
Bacillus subtilis possesses three homologous small cold shock proteins (CSPs; CspB, CspC, CspD, sequence identity >72%). They share a similar beta-sheet structure, as shown by circular dichroism, and have a very low conformational stability, with Csp
Autor:
Volker Sieber, Peter L. Graumann, Franz X. Schmid, Mohamed A. Marahiel, Thomas Schindler, Dieter Perl
Publikováno v:
Proteins: Structure, Function, and Genetics. 30:401-406
In the cold-shock protein CspB from Bacillus subtilis three exposed Phe residues (F15, F17, and F27) are essential for its function in binding to single-stranded nucleic acids. Usually, the hydrophobic Phe side chains are buried in folded proteins. W
Autor:
Franz X. Schmid, Dieter Perl
Publikováno v:
ChemInform. 33
Autor:
Dieter, Perl, Franz Xaver, Schmid
Publikováno v:
Chembiochem : a European journal of chemical biology. 3(1)