Examine the f1 complex of the atp synthase from bovine heart mitochondria. what prevents this f1 complex from rotating with the
f0 c-ring complex? examine the f1 complex of the atp synthase from bovine heart mitochondria. what prevents this f1 complex from rotating with the f0 c-ring complex? it is bound to the central stalk. nothing prevents it. the f1 complex rotates with the f0 c-ring complex. it is bound by the stator, which is connected to the stationary "a" subunit of f0. it is bound within the inner mitochondrial membrane.
By examining the F1 complex of ATP synthase which is from Bovine heart mitochondria. Then we should ask what prevents F1 complex from rotating with Fo c-ring complex?. It is bound to the central stalk. F1 rotates with Fo c-ring complex and nothing prevents it. The mitochondrial membrane is where Fo c-ring is bounded. Stationary "a" subunit of Fo is where the stator which is connected to it bounds. In conclusion, we will say that the answer is, it is bounded by the stator, which is corrected to the stationary "a" subunit of Fo. The ring-shaped C subunits form the rotor of the F1FO complex. FOF1 is bound to the central stalk, Therefore, it prevents it from rotation which is during the translocation of protons
PDCAAS takes into account both the amino acid profile and the DIGESTIBILITY of a protein. PDCAAS is majorly used to indicate the quality of a protein. Protein digestibility refers to the ability of a protein to be broken down so that it can be absorbed. Protein digestibility depends mainly on the source of the protein.<span />
