Answer:
This signifies that the protein primarily comprises multiple polypeptide chains connected together with the help of disulfide bonds. The enzymes may be found in the form of dimers, trimers, or tetramers. Various examples of dimers, trimers, and tetramer proteins are known, of them, NEMOs dimers are considered to be held by disulfide bonds.
Thus, it can be hypothesized that the enzyme under examination is a multimer held in combination by disulfide bonds, with each comprising catalytic sites. On breaking of disulfide bonds, the enzyme dissociates into its many single units.
This illustrates the reduction in catalytic activity. Each active site in a single unit will work, however, at a gradual rate. This also shows detection of multiple globular proteins after disulfide reduction.
Hey here is the answer,
It is a globular protein, it contains one iron atom, that can bind one oxygen molecule. Therefore it has high affinity for oxygen.
Hope this helps you...
Increases genetic variation, which in and of itself has extreme benefits such as protection against disease, capability to evolve, etc
An increase in the available water in an ecosystem would increase the sustainability of an ecosystem.
An increase of human interference can negatively impact local flora and fauna populations.
A decrease in the amount of sunlight would negative impact plants.
A decrease in the number of available producers will negatively impact the entire food chain/food web.
