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Avilov, SV; Aleksandrova, NA; Demchenko, AP
{ "URL": "https://aperta.ulakbim.gov.tr/record/93943", "abstract": "The interactions between an oligomeric heat-shock protein, alpha-crystallin, and its individual subunits with unfolded proteins were monitored by surface plasmon resonance. Immobilization at the sensor chip allowed us for the first time to study isolated alpha-crystallin subunits under physiological conditions. We observe that these subunits, in contrast to alpha-crystallin oligomers, do not bind unfolded protein. Our data indicate that quaternary structure of alpha-crystallin is necessary for its chaperone-like activity.", "author": [ { "family": "Avilov", "given": " SV" }, { "family": "Aleksandrova", "given": " NA" }, { "family": "Demchenko", "given": " AP" } ], "container_title": "PROTEIN AND PEPTIDE LETTERS", "id": "93943", "issue": "1", "issued": { "date-parts": [ [ 2004, 1, 1 ] ] }, "page": "41-48", "title": "Quaternary structure of alpha-crystallin is necessary for the binding of unfolded proteins: A surface plasmon resonance study", "type": "article-journal", "volume": "11" }
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