A recessive trait is observed when an organism has 2 recessive genetic factors.
Answer:
Thiamine pyrophosphate (derived from vitamin B1) is a coenzyme required for the activity of pyruvate dehydrogenase enzyme complex.
Explanation:
Pyruvate is the end product of glycolysis. During aerobic cellular respiration, pyruvate is oxidatively decarboxylated into acetyl CoA which in turn enters the Kreb's cycle. Oxidative decarboxylation of pyruvate is carried out by enzyme complex pyruvate dehydrogenase (PDH). The first step is simple decarboxylation and is catalyzed by pyruvate decarboxylase of the PDH complex.
The enzyme pyruvate decarboxylase and has a tightly bound coenzyme, thiamine pyrophosphate. Thiamine pyrophosphate is derived from vitamin B1. Lack of vitamin B1 in the human diet leads to beriberi that is characterized by an increased concentration of pyruvate in blood urine since oxidative decarboxylation cannot occur due to lack of the coenzyme thiamine pyrophosphate.
Answer:
Dung beetles lives in the animal dung and take nutrients from the undigested substances present in the dung. This dung is mixed with the soil by the beetle to increase the fertility of the soil. These nutrients is taken by plants with water through roots and makes their food in the form of carbohydrate from it in the process of photosynthesis. This carbohydrate is stored in different parts of plant body.
Answer:
True
explanation:
Hexadecimal numerals are widely used by computer system, designers and programmers.
Answer:
A series of nonpolar amino acids would most likely be located in the interior region of the tridimensional molecule.
Explanation:
Proteins are formed by linearly arranged amino acids, each with a side chain: the R-group.
Of the 20 different amino acids that compose the proteins, about half of them -10- are non-polar. Their R-groups are not stable if they are in contact with water, meaning that non-polar amino acids are hydrophobic.
When proteins are synthesized, they acquire a three-dimensional structure that makes them more stable. Lineal polypeptides get folded and turn into a shape that makes them more stable in the environment and capable of accomplishing their biological role. When they are in an aqueous media, their bent shape leaves the hydrophilic R-groups in contact with water. The hydrophilic R-groups stick in the center of the polypeptide, facing the protein interior, and avoiding interaction with water.
