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Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
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Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Published on: June 7, 2018

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ホリスマターゼメカニズムは,単一の保存されたタンパク質の折りたたみにおける根本的に異なるタイプの反応を明らかにする

Florian Hubrich1, Puneet Juneja2, Michael Müller1

  • 1Institute of Pharmaceutical Sciences, University of Freiburg , Albertstr. 25, 79104 Freiburg, Germany.

Journal of the American Chemical Society
|August 7, 2015
PubMed
まとめ

コリスマゼは薬学的可能性を持つ酵素である. この研究は,異なる反応機構を明らかにし,亜種に分類するために,コリスマターゼ亜種 (CH-FkbO,CH-Hyg5,CH-XanB2) を区別する主要なアミノ酸残基を特定した.

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