Related ArticlesNMR 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 47, 48 and 50 (all less than or equal to 0.07 ppm). Minimal changes were observed for NOEs associated with residues Val1 to His45. The weakening of some NOEs associated with the region Ala46-Ala50 may suggest a slightly increased flexibility for this region. Refinement of the previously calculated wild-type structures using distance constraints derived from the L48A mutant had little overall effect. Leu48-Ala50 is ill-defined for both wild-type and mutant proteins. These results suggest that Leu48 has no structural role and thus must be an important factor in the protein-receptor interface.
[NMR paper] Solution 1H NMR study of the active site molecular structure and magnetic properties
Solution 1H NMR study of the active site molecular structure and magnetic properties of the cyanomet complex of the isolated, tetrameric beta-chain from human adult hemoglobin.
Related Articles Solution 1H NMR study of the active site molecular structure and magnetic properties of the cyanomet complex of the isolated, tetrameric beta-chain from human adult hemoglobin.
Biochim Biophys Acta. 2004 Sep 1;1701(1-2):75-87
Authors: Tran AT, Kolczak U, La Mar GN
The solution molecular structure and the electronic and magnetic properties of the heme...
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[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.
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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] NMR studies on the solution structure of a deletion mutant of the transcarboxylase bi
NMR studies on the solution structure of a deletion mutant of the transcarboxylase biotin carrier subunit.
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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...
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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...
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[NMR paper] Determination of the NMR solution structure of a specific DNA complex of the Myb DNA-
Determination of the NMR solution structure of a specific DNA complex of the Myb DNA-binding domain.
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J Biomol NMR. 1995 Nov;6(3):294-305
Authors: Morikawa S, Ogata K, Sekikawa A, Sarai A, Ishii S, Nishimura Y, Nakamura H
The solution structure of a specific DNA complex of the minimum DNA-binding domain of the mouse c-Myb protein was determined by distance geometry calculations using a set of 1732 nuclear Overhauser enhancement...
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[NMR paper] Comparison of native and mutant proteins provides a sequence-specific assignment of t
Comparison of native and mutant proteins provides a sequence-specific assignment of the cysteinyl ligand proton NMR resonances in the 2 ferredoxin from Clostridium pasteurianum.
Related Articles Comparison of native and mutant proteins provides a sequence-specific assignment of the cysteinyl ligand proton NMR resonances in the 2 ferredoxin from Clostridium pasteurianum.
Biochemistry. 1994 Dec 6;33(48):14486-95
Authors: Scrofani SD, Brereton PS, Hamer AM, Lavery MJ, McDowall SG, Vincent GA, Brownlee RT, Hoogenraad NJ, Sadek M, Wedd AG
A...
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[NMR paper] Solution structure of human type-alpha transforming growth factor determined by heter
Solution structure of human type-alpha transforming growth factor determined by heteronuclear NMR spectroscopy and refined by energy minimization with restraints.
Related Articles Solution structure of human type-alpha transforming growth factor determined by heteronuclear NMR spectroscopy and refined by energy minimization with restraints.
Biochemistry. 1993 Jul 27;32(29):7334-53
Authors: Moy FJ, Li YC, Rauenbuehler P, Winkler ME, Scheraga HA, Montelione GT
Human type-alpha transforming growth factor (hTGF alpha) is a small mitogenic protein...
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[NMR paper] Solution structures of human transforming growth factor alpha derived from 1H NMR dat
Solution structures of human transforming growth factor alpha derived from 1H NMR data.
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Biochemistry. 1990 Aug 28;29(34):7805-13
Authors: Kline TP, Brown FK, Brown SC, Jeffs PW, Kopple KD, Mueller L
The 600-MHz 1H NMR spectrum of the des-Val-Val mutant of human transforming growth factor alpha (TGF-alpha) was reassigned at pH = 6.3. The conformation space of des-Val-Val TGF-alpha was explored by distance geometry embedding followed by...
NMR study on solution structure of the site-specific mutant Leu48----Ala transforming
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