Zobrazeno 1 - 10
of 64
pro vyhledávání: '"Ribonuclease T"'
Autor:
Daniel A. Nissley, Mai Suan Li, Quyen Vu Van, Yang Jiang, Ian Sitarik, Edward P. O'Brien, Lan Pham Dang
Synonymous mutations in messenger RNAs (mRNAs) can reduce protein-protein binding affinities by more than half despite leaving the protein’s amino acid sequence unaltered. Here, we use coarse-grain simulations of protein synthesis, ejection from th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c3e2e97dce693e5bd5ef1648be103d62
https://doi.org/10.1101/2021.10.26.465867
https://doi.org/10.1101/2021.10.26.465867
Publikováno v:
Journal of Molecular Biology. 285:829-842
The rate-limiting step during the refolding of S54G/P55N ribonuclease T1 is determined by the slow trans-->cis prolyl isomerisation of Pro39. We investigated the refolding of this variant by one-dimensional (1D) and two-dimensional (2D) real-time NMR
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::941c3ae11735b9858cb42604b66710fe
https://doi.org/10.1006/jmbi.1998.2364
https://doi.org/10.1006/jmbi.1998.2364
Publikováno v:
Journal of Molecular Biology. 275:651-661
His92 of Ribonuclease T1 combines functional and structural features involving both imidazole nitrogens. To evaluate the use of Asn and Gln substitutions in dissecting the properties of histidines, we analysed the consequences of the His92Gln and His
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1206c5426c3bfe5b5b98ae6b95453ac5
https://doi.org/10.1006/jmbi.1997.1480
https://doi.org/10.1006/jmbi.1997.1480
Publikováno v:
Journal of Molecular Biology. 266:400-423
Limits of NMR structure determination using multidimensional NMR spectroscopy, variable target function calculations and relaxation matrix analysis were explored using the model protein ribonuclease T1(RNase T1). The enzyme consists of 104 amino acid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::daf598b7775c357c7f4d3a2e6c7d90b3
https://doi.org/10.1006/jmbi.1996.0784
https://doi.org/10.1006/jmbi.1996.0784
Publikováno v:
Journal of Molecular Biology. 245:69-78
In wild-type ribonuclease T1 the peptide bond between Tyr38 and Pro39 is in the cis conformation. When Pro39 is replaced by an alanine this cis conformation is retained, and a non-prolyl cis Tyr38-Ala39 peptide bond is generated. We employed a stoppe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2b3c61457d62e5ab6b5936727581ee0a
https://doi.org/10.1016/s0022-2836(95)80039-5
https://doi.org/10.1016/s0022-2836(95)80039-5
Publikováno v:
Enzyme and Microbial Technology. 16:281-285
Nonradioactive immunoassays incorporating an element of amplification in their detection system require the use of components that are highly purified. Flavin adenine dinucleotide-3′-phosphate (FADP) is the primary substrate used in such an amplifi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::506791b2b292336a52de0ef7f672b798
https://doi.org/10.1016/0141-0229(94)90167-8
https://doi.org/10.1016/0141-0229(94)90167-8
Autor:
Wolfram Saenger, Ulrich Hahn, Heinz Fabian, Christian P. Schultz, Olfert Landt, Dieter Naumann
Publikováno v:
Journal of Molecular Biology. 232:967-981
Max-Delbruck-Centrum fur Molekulare Medizin Robert-Rossle-Strase 10, D-1115 Berlin-Buch, Germany; Robert-Koch Institut des Bundesgesundheitsamtes Nordufer 20, D-1000 Berlin 65, Germany and Institut fur Kristallographie der Freien Universitat Berlin T
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::749d814d612c5a321f2453392f376d24
https://doi.org/10.1006/jmbi.1993.1442
https://doi.org/10.1006/jmbi.1993.1442
Autor:
Shouting Huang, Murray P. Deutscher
Publikováno v:
Journal of Biological Chemistry. 267:25609-25613
The Escherichia coli rnt gene encoding the enzyme RNase T, which is responsible for the end-turnover of tRNA, was cloned on a 1.5-kilobase DNA fragment. When placed in pUC18 and pUC19 vectors this fragment led to approximately a 40-fold overexpressio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::508c392df8abc46c3af17835e41d212e
https://doi.org/10.1016/s0021-9258(19)74084-8
https://doi.org/10.1016/s0021-9258(19)74084-8
Autor:
Gertraud Koellner, Hui-Woog Choe, Wolfram Saenger, Ulrich Hahn, A. Zouni, Udo Heinemann, Hans-Peter Grunert
Publikováno v:
Journal of Molecular Biology. 224:701-713
In the genetically mutated ribonuclease T1 His92Ala (RNase T1 His92Ala), deletion of the active site His92 imidazole leads to an inactive enzyme. Attempts to crystallize RNase T1 His92Ala under conditions used for wild-type enzyme failed, and a modif
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::59df2ab54053a8eb44649974bc4b8538
https://doi.org/10.1016/0022-2836(92)90554-w
https://doi.org/10.1016/0022-2836(92)90554-w
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1078:307-312
The structure of RNase F 1 in aqueous solution has been studied by Raman spectroscopy and compared with that of a homologous enzyme, RNase T 1 . RNase F 1 contains less β-sheet and α-helical structure and more irregular structure than RNase T 1 . T
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4f8414bb221af7334626e8a9377cfe5e
https://doi.org/10.1016/0167-4838(91)90148-s
https://doi.org/10.1016/0167-4838(91)90148-s