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pH dependence of stability of the wild-type tryptophan synthase alpha-subunit and two mutant proteins (Glu49 replaced by Met or Gln).

作者信息

Yutani K, Ogasahara K, Sugino Y

出版信息

J Mol Biol. 1980 Dec 25;144(4):455-65. doi: 10.1016/0022-2836(80)90331-9.

DOI:10.1016/0022-2836(80)90331-9
PMID:7019448
Abstract
摘要

相似文献

1
pH dependence of stability of the wild-type tryptophan synthase alpha-subunit and two mutant proteins (Glu49 replaced by Met or Gln).野生型色氨酸合酶α亚基及两种突变蛋白（谷氨酸49被甲硫氨酸或谷氨酰胺取代）稳定性的pH依赖性
J Mol Biol. 1980 Dec 25;144(4):455-65. doi: 10.1016/0022-2836(80)90331-9.
2
Comparison of denaturation by guanidine hydrochloride of the wild type tryptophan synthase alpha-subunit of Escherichia coli and two mutant protein (Glu 49 replaced by Met or Gln).
J Biochem. 1979 Apr;85(4):915-21. doi: 10.1093/oxfordjournals.jbchem.a132423.
3
Comparison of CD spectra in the aromatic region on a series of variant proteins substituted at a unique position of tryptophan synthase alpha-subunit.对一系列在色氨酸合酶α亚基独特位置进行取代的变体蛋白质在芳香族区域的圆二色光谱进行比较。
Proteins. 1989;5(3):211-7. doi: 10.1002/prot.340050304.
4
Refolding and reactivation of Escherichia coli tryptophan synthase beta2 subunit after inactivation and dissociation in guanidine hydrochloride at acidic pH.
Eur J Biochem. 1978 Dec;92(2):437-41. doi: 10.1111/j.1432-1033.1978.tb12764.x.
5
Evidence that glutamic acid 49 of tryptophan synthase alpha subunit is a catalytic residue. Inactive mutant proteins substituted at position 49 bind ligands and transmit ligand-dependent to the beta subunit.
J Biol Chem. 1988 Jun 25;263(18):8611-4.
6
Effect of amino acid residues on conformational stability in eight mutant proteins variously substituted at a unique position of the tryptophan synthase alpha-subunit.
J Biol Chem. 1984 Nov 25;259(22):14076-81.
7
Effect of single amino acid substitutions on the protease susceptibility of tryptophan synthase alpha subunit.
Eur J Biochem. 1985 Jul 1;150(1):17-21. doi: 10.1111/j.1432-1033.1985.tb08979.x.
8
Effect of a single amino acid substitution on the near-ultraviolet CD spectra of tryptophan synthase alpha-subunit.单个氨基酸取代对色氨酸合酶α亚基近紫外圆二色光谱的影响。
J Biochem. 1980 Jan;87(1):117-21. doi: 10.1093/oxfordjournals.jbchem.a132716.
9
Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase alpha subunit.在色氨酸合酶α亚基的一个独特位置被取代的一系列变体蛋白中，构象稳定性对氨基酸残基疏水性的依赖性。
Proc Natl Acad Sci U S A. 1987 Jul;84(13):4441-4. doi: 10.1073/pnas.84.13.4441.
10
Equilibrium and kinetic analyses of unfolding and refolding for the conserved proline mutants of tryptophan synthase alpha subunit.色氨酸合成酶α亚基保守脯氨酸突变体的去折叠和重折叠的平衡及动力学分析。
Biochemistry. 1997 Jan 28;36(4):932-40. doi: 10.1021/bi961660c.

引用本文的文献

1
Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase alpha subunit.在色氨酸合酶α亚基的一个独特位置被取代的一系列变体蛋白中，构象稳定性对氨基酸残基疏水性的依赖性。
Proc Natl Acad Sci U S A. 1987 Jul;84(13):4441-4. doi: 10.1073/pnas.84.13.4441.