Title : ATP hydrolysis induces an intermediate conformational state in GroEL.

Pub. Date : 1999 Jan

PMID : 9914513






3 Functional Relationships(s)
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1 In addition, ATP induces a conformational change in GroEL characterized by (a) the appearance of a reversible low temperature endotherm in the DSC profiles of the protein, and (b) an enhanced binding of the hydrophobic probe 8-anilino-naphthalene-1-sulfonate (ANS), which strictly depends on ATP hydrolysis. 8-anilino-1-naphthalenesulfonic acid heat shock protein family D (Hsp60) member 1 Homo sapiens
2 In addition, ATP induces a conformational change in GroEL characterized by (a) the appearance of a reversible low temperature endotherm in the DSC profiles of the protein, and (b) an enhanced binding of the hydrophobic probe 8-anilino-naphthalene-1-sulfonate (ANS), which strictly depends on ATP hydrolysis. 8-anilino-1-naphthalenesulfonic acid heat shock protein family D (Hsp60) member 1 Homo sapiens
3 The similar sensitivity to K+ of the temperature range where activation of the GroEL ATPase activity, the low temperature endotherm, and the increase of the ANS fluorescence are abserved strongly indicates the existence of a conformational state of GroEL during ATP hydrolysis, different from that generated on ADP or AMP-PNP binding. 8-anilino-1-naphthalenesulfonic acid heat shock protein family D (Hsp60) member 1 Homo sapiens