Entropic Stabilization of the Tryptophan Synthase α-Subunit from a Hyperthermophile, Pyrococcus furiosus-Reference-Cited by-同舟云学术

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Entropic Stabilization of the Tryptophan Synthase α-Subunit from a Hyperthermophile, Pyrococcus furiosus

Published:2001-04 Issue:14 Volume:276 Page:11062-11071
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Yamagata Yuriko,Ogasahara Kyoko,Hioki Yusaku,Lee Soo Jae,Nakagawa Atsushi,Nakamura Haruki,Ishida Masami,Kuramitsu Seiki,Yutani Katsuhide

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference76 articles.

1. Tryptophan Synthase

2. Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium.

3. Preliminary X-Ray Diffraction Study of the Wild-Type and a Mutationally-Altered Tryptophan Synthetase alpha Subunit

4. X-ray crystal structures of the oxidized and reduced forms of the rubredoxin from the marine hyperthermophilic archaebacterium pyrococcus furiosus

5. Structure of a Hyperthermophilic Tungstopterin Enzyme, Aldehyde Ferredoxin Oxidoreductase

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2. Evaluating the strengths of salt bridges in the CutA1 protein using molecular dynamic simulations: a comparison of different force fields;FEBS Open Bio;2019-09-27

3. Conservation of the structure and function of bacterial tryptophan synthases;IUCrJ;2019-05-29

4. Confirmation of the formation of salt bridges in the denatured state of CutA1 protein using molecular dynamics simulations;Biophysics and Physicobiology;2019

5. Ion–ion interactions in the denatured state contribute to the stabilization of CutA1 proteins;Scientific Reports;2018-05-16

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