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Background: The 70 kDa heat shock proteins (Hsp70) are a family of molecular chaperones, which promote protein folding and participate in many cellular functions. The Hsp70 chaperones are composed of two major domains. The N-terminal ATPase domain binds to and hydrolyzes ATP, whereas the C-terminal domain is required for polypeptide binding. Cooperation of both domains is needed for protein folding...
Background: Proton-translocating ATP synthases convert the energy generated from photosynthesis or respiration into ATP. These enzymes, termed F 0 F 1 -ATPases, are structurally highly conserved. In Escherichia coli, F 0 F 1 -ATPase consists of a membrane portion, F 0 , made up of three different polypeptides (a, b and c) and an F 1 portion comprising...
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