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α-Crystallin binds to the aggregation-prone molten-globule state of alkaline protease: Implications for preventing irreversible thermal denaturation

α-Crystallin, the major eye-lens protein with sequence homology with heat-shock proteins (HSPs), acts like a molecular chaperone by suppressing the aggregation of damaged crystallins and proteins. To gain more insight into its chaperoning ability, we used a protease as the model system that is known...

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Main Authors: Tanksale, Aparna, Ghatge, Mohini, Deshpande, Vasanti
Formato: Artigo
Idioma:Inglês
Publicado: Cold Spring Harbor Laboratory Press 2002
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Acceso en liña:https://ncbi.nlm.nih.gov/pmc/articles/PMC2384148/
https://ncbi.nlm.nih.gov/pubmed/12070325
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