Related ArticlesComplete assignments of magnetic resonances of ribonuclease H from Escherichia coli by double- and triple-resonance 2D and 3D NMR spectroscopies.
Biochemistry. 1993 Jun 1;32(21):5656-69
Authors: Yamazaki T, Yoshida M, Nagayama K
Assignments of 1H, 15N, and 13C magnetic resonances for ribonuclease H from Escherichia coli have been completed using double- and triple-resonance 2D and 3D NMR experiments. These assignments include all types of 1H, 15N, and 13C nuclei detectable by NMR. The enzyme used, which cleaves the RNA moiety of an RNA-DNA duplex, consists of 155 amino acid residues and has 1962 nuclei (227 nitrogen, 762 carbons, and 973 protons) observable independently by NMR. Among those, 1868 nuclei (95%) have been assigned. Two methods, 3D HCH and 13C-13C-1H heteroSQC/homoSQC, were newly devised to complete the side chain assignments. These methods were used to elucidate the -CH2- and -C-CH-substructures. Triple-resonance experiments to detect other types of substructures, (e.g., -N-CH- and -C-NH-) were also applied. In total, 10 kinds of 3D NMR experiments were used to complete the assignments. The chemical shifts obtained through the assignments were analyzed in terms of the tertiary structure of the protein molecule. Among the 13C chemical shifts, larger secondary shifts (deviations from shifts at the random coil state) were observed for the C alpha, C beta, and C' nuclei, which reflect the local structures on the backbone, that is, the alpha-helix, beta-sheet, and left-handed helix, respectively.
(1)H, (13)C and (15)N NMR assignments of the Escherichia coli Orf135 protein.
(1)H, (13)C and (15)N NMR assignments of the Escherichia coli Orf135 protein.
(1)H, (13)C and (15)N NMR assignments of the Escherichia coli Orf135 protein.
Biomol NMR Assign. 2011 May 7;
Authors: Kawasaki K, Yoneyama M, Murata-Kamiya N, Harashima H, Kojima C, Ito Y, Kamiya H, Mishima M
Escherichia coli Orf135 protein is thought to be an enzyme that efficiently hydrolyzes oxidatively damaged nucleotides such as 2-hydroxy-dATP, 8-hydroxy-dGTP and 5-hydroxy-CTP, in addition to 5-methyl-dCTP, dCTP and CTP, thus preventing mutations in cells caused by...
nmrlearner
Journal club
0
05-10-2011 05:11 PM
[NMR paper] Acid-induced denaturation of Escherichia coli ribonuclease HI analyzed by CD and NMR
Acid-induced denaturation of Escherichia coli ribonuclease HI analyzed by CD and NMR spectroscopies.
Related Articles Acid-induced denaturation of Escherichia coli ribonuclease HI analyzed by CD and NMR spectroscopies.
Biopolymers. 2003 Jun;69(2):176-88
Authors: Yamasaki K, Yamasaki T, Kanaya S, Oobatake M
Acid-induced denaturation of the ribonuclease HI protein from Escherichia coli was analyzed by CD and NMR spectroscopies. The CD measurement revealed that the acid denaturation at 10 degrees C proceeds from the native state (N-state) to a...
nmrlearner
Journal club
0
11-24-2010 09:01 PM
[NMR paper] NMR structure of ribonuclease HI from Escherichia coli.
NMR structure of ribonuclease HI from Escherichia coli.
Related Articles NMR structure of ribonuclease HI from Escherichia coli.
Biol Pharm Bull. 2000 Oct;23(10):1147-52
Authors: Fujiwara M, Kato T, Yamazaki T, Yamasaki K, Nagayam K
The solution structure of ribonuclease HI (RNase HI) from Escherichia coli (E. coli), a protein of 155 residues, was determined. Three-dimensional nuclear Overhauser enhancement spectroscopy (NOESY) was used to obtain 1,424 distance constraints between individually assigned polypeptide chain hydrogen atoms....
nmrlearner
Journal club
0
11-19-2010 08:29 PM
[NMR paper] Pressure-denatured state of Escherichia coli ribonuclease HI as monitored by Fourier
Pressure-denatured state of Escherichia coli ribonuclease HI as monitored by Fourier transform infrared and NMR spectroscopy.
Related Articles Pressure-denatured state of Escherichia coli ribonuclease HI as monitored by Fourier transform infrared and NMR spectroscopy.
Biochemistry. 1998 Dec 22;37(51):18001-9
Authors: Yamasaki K, Taniguchi Y, Takeda N, Nakano K, Yamasaki T, Kanaya S, Oobatake M
Pressure denaturation of Escherichia coli ribonuclease HI (RNase HI) was studied by Fourier transform infrared (FTIR) and two-dimensional NMR...
nmrlearner
Journal club
0
11-17-2010 11:15 PM
[NMR paper] NMR assignments, secondary structure and hydration of oxidized Escherichia coli flavo
NMR assignments, secondary structure and hydration of oxidized Escherichia coli flavodoxin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles NMR assignments, secondary structure and hydration of oxidized Escherichia coli flavodoxin.
Eur J Biochem. 1997 Mar 1;244(2):384-99
Authors: Ponstingl H, Otting G
Recombinant flavodoxin from Escherichia coli was uniformly enriched with 15N and 13C isotopes and its oxidized form in aqueous...
nmrlearner
Journal club
0
08-22-2010 03:03 PM
[NMR paper] Glutaredoxin-3 from Escherichia coli. Amino acid sequence, 1H AND 15N NMR assignments
Glutaredoxin-3 from Escherichia coli. Amino acid sequence, 1H AND 15N NMR assignments, and structural analysis.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_full_free.gif Related Articles Glutaredoxin-3 from Escherichia coli. Amino acid sequence, 1H AND 15N NMR assignments, and structural analysis.
J Biol Chem. 1996 Mar 22;271(12):6736-45
Authors: Aslund F, Nordstrand K, Berndt KD, Nikkola M, Bergman T, Ponstingl H, Jörnvall H, Otting G, Holmgren A
The primary and...
nmrlearner
Journal club
0
08-22-2010 02:27 PM
[NMR paper] Folding pathway of Escherichia coli ribonuclease HI: a circular dichroism, fluorescen
Folding pathway of Escherichia coli ribonuclease HI: a circular dichroism, fluorescence, and NMR study.
Related Articles Folding pathway of Escherichia coli ribonuclease HI: a circular dichroism, fluorescence, and NMR study.
Biochemistry. 1995 Dec 26;34(51):16552-62
Authors: Yamasaki K, Ogasahara K, Yutani K, Oobatake M, Kanaya S
The unfolding and refolding processes of Escherichia coli ribonuclease HI at 25 degrees C, induced by concentration jumps of either guanidine hydrochloride (GuHCl) or urea, were investigated using stopped-flow...
nmrlearner
Journal club
0
08-22-2010 03:50 AM
[NMR paper] Sequence-specific NMR assignments of the trp repressor from Escherichia coli using th
Sequence-specific NMR assignments of the trp repressor from Escherichia coli using three-dimensional 15N/1H heteronuclear techniques.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Sequence-specific NMR assignments of the trp repressor from Escherichia coli using three-dimensional 15N/1H heteronuclear techniques.
Eur J Biochem. 1992 Feb 15;204(1):137-46
Authors: Borden KL, Bauer CJ, Frenkiel TA, Beckmann P, Lane AN
...