Hydrogen/Deuterium Exchange Behavior During Denaturing/Refolding Processes Determined in Tetragonal Hen Egg-White Lysozyme Crystals.

Szczegóły
Abstrakt

Tytuł:: Hydrogen/Deuterium Exchange Behavior During Denaturing/Refolding Processes Determined in Tetragonal Hen Egg-White Lysozyme Crystals.
Autorzy:: Kita A; Institute for Integrated Radiation and Nuclear Science, Kyoto University, Kumatori, Sen-nan, Osaka, 590-0494, Japan.
Morimoto Y; Institute for Integrated Radiation and Nuclear Science, Kyoto University, Kumatori, Sen-nan, Osaka, 590-0494, Japan. .
Źródło:: Molecular biotechnology [Mol Biotechnol] 2022 May; Vol. 64 (5), pp. 590-597. Date of Electronic Publication: 2022 Jan 13.
Typ publikacji:: Journal Article
Język:: English
Imprint Name(s):: Publication: [Cham] : Springer
Original Publication: Totowa, NJ : Humana Press, c1994-
MeSH Terms:: Hydrogen*/chemistry
Muramidase*
Animals ; Chickens/metabolism ; Deuterium/chemistry ; Protein Denaturation ; Proteins ; Solvents
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Grant Information:: Ishizue Kyoto University; 2020 Kyoto University
Contributed Indexing:: Keywords: Crystal structure; Denatured/refolded protein; H/D exchange; Hen egg-white lysozyme; X/N joint refinement
Substance Nomenclature:: 0 (Proteins)
0 (Solvents)
7YNJ3PO35Z (Hydrogen)
AR09D82C7G (Deuterium)
EC 3.2.1.17 (Muramidase)
Entry Date(s):: Date Created: 20220114 Date Completed: 20220426 Latest Revision: 20220426
Update Code:: 20240104
DOI:: 10.1007/s12033-022-00447-7
PMID:: 35028904
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The hydrogen/deuterium (H/D) exchange of main-chain amide hydrogens in the protein that denatured and refolded in deuterated solvent is considered to contain the traces of hydrogen bond cleavages or the exposure to solvent of the buried part of the protein during the denaturing and refolding (denaturing/refolding) processes. Here, we report the H/D exchange behaviors in hen egg-white lysozymes denatured under acidic conditions, basic conditions, and thermal conditions and then refolded in deuterated solvents, using crystallographic methods. The results indicate that the space containing the Trp28 side chain was hardly exposed to the solvent in acidic conditions, but exposed under basic or heated conditions. Moreover, the β-bridges between Tyr53 and Ile58 in strands β2 and β3, which are in a highly conserved region, show some tolerance to changes in pD. The results indicate that crystallographic method is one of the powerful tools to analyze the denaturing/refolding processes of proteins.
(© 2022. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.)

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