Inhibitor and substrate binding induced stability of HIV-1 protease against sequential dissociation and unfolding revealed by high pressure spectroscopy and kinetics.

Inhibitor and substrate binding induced stability of HIV-1 protease against sequential dissociation and unfolding revealed by high pressure spectroscopy and kinetics.

High-pressure methods have become an interesting tool of investigation of structural stability of proteins. They are used to study protein unfolding, but dissociation of oligomeric proteins can be addressed this way, too. HIV-1 protease, although an interesting object of biophysical experiments, has...

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Bibliographic Details
Main Authors: Marek Ingr, Reinhard Lange, Věra Halabalová, Alaa Yehya, Josef Hrnčiřík, Dominique Chevalier-Lucia, Laetitia Palmade, Claire Blayo, Jan Konvalinka, Eliane Dumay
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2015-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC4362767?pdf=render

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http://europepmc.org/articles/PMC4362767?pdf=render

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