Related ArticlesNMR studies on the solution structure of a deletion mutant of the transcarboxylase biotin carrier subunit.
Int J Biol Macromol. 2002 Oct 1;30(5):233-42
Authors: Jank MM, Sadowsky JD, Peikert C, Berger S
A deletion mutant of the transcarboxylase biotin carrier protein was completely labeled with 13C and 15N. A multitude of 2D and 3D NMR spectra were recorded and assigned. An NMR solution structure was derived from the data and compared in detail with the recently published structure of the wild-type. It is shown that deletion of 30% of the amino acids does not alter the structure of the rigid protein core.
[NMR paper] The NMR solution structure of a mutant of the Max b/HLH/LZ free of DNA: insights into
The NMR solution structure of a mutant of the Max b/HLH/LZ free of DNA: insights into the specific and reversible DNA binding mechanism of dimeric transcription factors.
Related Articles The NMR solution structure of a mutant of the Max b/HLH/LZ free of DNA: insights into the specific and reversible DNA binding mechanism of dimeric transcription factors.
J Mol Biol. 2004 Sep 17;342(3):813-32
Authors: Sauvé S, Tremblay L, Lavigne P
Basic region-helix1-loop-helix2-leucine zipper (b/H(1)LH(2)/LZ) transcription factors bind specific DNA sequence...
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[NMR paper] Characterization of the carboxylate delivery module of transcarboxylase: following sp
Characterization of the carboxylate delivery module of transcarboxylase: following spontaneous decarboxylation of the 1.3S-CO2- subunit by NMR and FTIR spectroscopies.
Related Articles Characterization of the carboxylate delivery module of transcarboxylase: following spontaneous decarboxylation of the 1.3S-CO2- subunit by NMR and FTIR spectroscopies.
Biochemistry. 2002 Feb 19;41(7):2191-7
Authors: Rivera-Hainaj RE, Pusztai-Carey M, Venkat Reddy D, Choowongkomon K, Sönnichsen FD, Carey PR
Transcarboxylase (TC) is a multisubunit enzyme that...
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11-24-2010 08:49 PM
[NMR paper] Solid-state NMR studies of the secondary structure of a mutant prion protein fragment
Solid-state NMR studies of the secondary structure of a mutant prion protein fragment of 55 residues that induces neurodegeneration.
Related Articles Solid-state NMR studies of the secondary structure of a mutant prion protein fragment of 55 residues that induces neurodegeneration.
Proc Natl Acad Sci U S A. 2001 Sep 25;98(20):11686-90
Authors: Laws DD, Bitter HM, Liu K, Ball HL, Kaneko K, Wille H, Cohen FE, Prusiner SB, Pines A, Wemmer DE
The secondary structure of a 55-residue fragment of the mouse prion protein, MoPrP(89-143), was studied in...
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[NMR paper] Studies on solution NMR structure of brazzein : Secondary structure and molecular sca
Studies on solution NMR structure of brazzein : Secondary structure and molecular scaffold.
Related Articles Studies on solution NMR structure of brazzein : Secondary structure and molecular scaffold.
Sci China C Life Sci. 1999 Aug;42(4):409-19
Authors: Gao G, Dai J, Ding M, Hellekant G, Wang J, Wang D
Brazzein is a sweet-tasting protein isolated from the fruit of West African plantPentadiplandra brazzeana Baillon. It is the smallest and the most water-soluble sweet protein discovered so far and is highly thermostable. The proton NMR study of...
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11-18-2010 08:31 PM
Solution NMR structure of the V27A drug resistant mutant of influenza A M2 channel.
Solution NMR structure of the V27A drug resistant mutant of influenza A M2 channel.
Solution NMR structure of the V27A drug resistant mutant of influenza A M2 channel.
Biochem Biophys Res Commun. 2010 Sep 9;
Authors: Pielak RM, Chou JJ
The M2 protein of influenza A virus forms a proton-selective channel that is required for viral replication; it is also the target of the anti-influenza drugs, amantadine and rimantadine. Widespread drug-resistant mutants, however, has greatly compromised the effectiveness of these drugs. Here, we report the...
[NMR paper] NMR study on solution structure of the site-specific mutant Leu48----Ala transforming
NMR study on solution structure of the site-specific mutant Leu48----Ala transforming growth factor alpha.
Related Articles NMR study on solution structure of the site-specific mutant Leu48----Ala transforming growth factor alpha.
Int J Pept Protein Res. 1992 Feb;39(2):111-6
Authors: Kline TP, Mueller L
The NMR spectra of the Leu48----Ala mutant of human transforming growth factor alpha were compared to that of the wild-type. All chemical shift changes are less than or equal to 0.02 ppm with the exception of resonances associated with residues...
NMR studies on the solution structure of a deletion mutant of the transcarboxylase bi
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