Related ArticlesFluctuations in free or substrate-complexed lysozyme and a mutant of it detected on x-ray crystallography and comparison with those detected on NMR.
J Biochem. 2002 May;131(5):701-4
Authors: Ohmura T, Motoshima H, Ueda T, Imoto T
A mutant lysozyme in which Arg14 and His15 were deleted together exhibited higher activity toward glycol chitin than the wild-type lysozyme. Moreover, the mutant lysozyme, which is less stable than the wild-type lysozyme by 7 degrees C, showed a shift of temperature dependence of activity to the low temperature side compared with the wild-type lysozyme [Protein Eng. 7, 743-748 (1994)]. In the free enzyme, the internal motion of the mutant lysozyme was similar to that of the wild-type. The internal motions of the wild-type and mutant lysozymes in the enzyme-substrate complex increased more than those in the free enzymes. Moreover, the increased internal motions of the substrate-complexed mutant lysozyme were greater than those of the substrate-complexed wild-type lysozyme in several residues [J. Mol. Biol. 286, 1547-1565 (1999)]. The structure of the mutant lysozyme was very similar to that of the wild-type lysozyme. Both structures were also alike in the complex of the trimer of N-acetyl-D-glucosamine. The mobility from B-factors agreed to some degree with that from order parameters in the regions showing great mobility of the protein, but this was not the case in the regions showing fast motion. However, we came to the same conclusion that the increased activity of the mutant lysozyme is due to the increase in the fluctuation of the lysozyme molecule. B-factor and order parameter do not always exhibit harmony because the time-scale of the analysis of mobility is different. However, they are not incompatible but complementary for detecting precise protein motions.
Influence of substrate modification and C-terminal truncation on the active site structure of substrate-bound heme oxygenase from Neisseriae meningitidis; A 1H NMR study.
Influence of substrate modification and C-terminal truncation on the active site structure of substrate-bound heme oxygenase from Neisseriae meningitidis; A 1H NMR study.
Influence of substrate modification and C-terminal truncation on the active site structure of substrate-bound heme oxygenase from Neisseriae meningitidis; A 1H NMR study.
Biochemistry. 2011 Aug 27;
Authors: Peng D, Satterlee JD, Ma LH, Dallas JL, Smith KM, Zhang X, Sato M, La Mar GN
Abstract
Heme oxygenase, HO, from the pathogenic bacterium N. meningitidis, NmHO, which...
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Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexes.
Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexes.
Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexes.
J Inorg Biochem. 2010 Oct;104(10):1063-70
Authors: Du Z, Unno M, Matsui T, Ikeda-Saito M, La Mar GN
Proton 2D NMR was used to confirm in solution a highly conserved portion of the molecular structure upon substrate loss for the...
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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.
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] Dynamic properties of the G93A mutant of copper-zinc superoxide dismutase as detected
Dynamic properties of the G93A mutant of copper-zinc superoxide dismutase as detected by NMR spectroscopy: implications for the pathology of familial amyotrophic lateral sclerosis.
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Biochemistry. 2003 Feb 25;42(7):1890-9
Authors: Shipp EL, Cantini F, Bertini I, Valentine JS, Banci L
The backbone assignment of the copper-zinc superoxide dismutase...
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[NMR paper] Flexibility and ligand exchange in a buried cavity mutant of T4 lysozyme studied by m
Flexibility and ligand exchange in a buried cavity mutant of T4 lysozyme studied by multinuclear NMR.
Related Articles Flexibility and ligand exchange in a buried cavity mutant of T4 lysozyme studied by multinuclear NMR.
Biochemistry. 2000 Oct 17;39(41):12614-22
Authors: Mulder FA, Hon B, Muhandiram DR, Dahlquist FW, Kay LE
The Leu99-->Ala mutant of T4 lysozyme contains a large internal cavity in the core of its C-terminal domain that is capable of reversibly binding small hydrophobic compounds. Although the cavity is completely buried,...
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[NMR paper] Local fluctuations and global unfolding of partially folded BPTI detected by NMR.
Local fluctuations and global unfolding of partially folded BPTI detected by NMR.
Related Articles Local fluctuations and global unfolding of partially folded BPTI detected by NMR.
Biophys Chem. 1997 Feb 28;64(1-3):45-57
Authors: Barbar E, LiCata VJ, Barany G, Woodward C
The protein Abu is a chemically synthesized variant of bovine pancreatic trypsin inhibitor (BPTI) with the 14-38 disulfide bond intact and cysteines 5, 30, 51, and 55 replaced by alpha-amino-n-butyric acid (Abu). At 1-6 degrees C and pH 4.5-6.5, Abu is partially folded with a...
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[NMR paper] Local fluctuations and global unfolding of partially folded BPTI detected by NMR.
Local fluctuations and global unfolding of partially folded BPTI detected by NMR.
Related Articles Local fluctuations and global unfolding of partially folded BPTI detected by NMR.
Biophys Chem. 1997 Feb 28;64(1-3):45-57
Authors: Barbar E, LiCata VJ, Barany G, Woodward C
The protein Abu is a chemically synthesized variant of bovine pancreatic trypsin inhibitor (BPTI) with the 14-38 disulfide bond intact and cysteines 5, 30, 51, and 55 replaced by alpha-amino-n-butyric acid (Abu). At 1-6 degrees C and pH 4.5-6.5, Abu is partially folded with a...
Fluctuations in free or substrate-complexed lysozyme and a mutant of it detected on x
Linear Mode
