Answer:the fitness of an organism is the ability to survive and reproduce
Explanation:
Answer:
Bridgham et al. (2006) showed that the interaction between a steroid hormone (aldosterone-M) and its receptor (mineralocorticoid) evolved by Darwinian gradualism. In this work, the authors demonstrated a primitive affinity between the hormone and its receptor that was initially present in chemically similar but more ancient ligands. This result has implications in understanding the association between gene duplication and the evolution of hormone signaling pathways. For example, in invertebrates, this work reinforces the importance of gene duplication in the existing interaction between paralogous glucocorticoid receptors and their receptor mineralocorticoid genes that were derived from duplication (Thornton 2001).
The publications above cited are the following:
J.T. Bridgham, S.M. Carroll, and J.W. Thornton (2006). Evolution of hormone-receptor complexity by molecular exploitation. Science, 312(5770), 97-101.
JW Thornton. Evolution of vertebrate steroid receptors from an ancestral estrogen receptor by ligand exploitation and serial genome expansions, Proc Natl Acad Sci USA (PNAS), 2001, vol. 98 10 (pg. 5671-5676).
Answer:
Mining
Explanation:
The other three natural ways of helping replenish the environment.
I believe the answer is restriction organism.
Answer:Recall that the glycolytic pathway generates NADH in the cytosol in the oxidation of glyceraldehyde 3-phosphate, and NAD+ must be regenerated for glycolysis to continue. How is cytosolic NADH reoxidized under aerobic conditions? NADH cannot simply pass into mitochondria for oxidation by the respiratory chain, because the inner mitochondrial membrane is impermeable to NADH and NAD+. The solution is that electrons from NADH, rather than NADH itself, are carried across the mitochondrial membrane. One of several means of introducing electrons from NADH into the electron transport chain is the glycerol 3-phosphate shuttle (Figure 18.37). The first step in this shuttle is the transfer of a pair of electrons from NADH to dihydroxyacetone phosphate, a glycolytic intermediate, to form glycerol 3-phosphate.This reaction is catalyzed by a glycerol 3-phosphate dehydrogenase in the cytosol. Glycerol 3-phosphate is reoxidized to dihydroxyacetone phosphate on the outer surface of the inner mitochondrial membrane by a membrane-bound isozyme of glycerol 3-phosphate dehydrogenase. An electron pair from glycerol 3-phosphate is transferred to a FAD prosthetic group in this enzyme to form FADH2. This reaction also regenerates dihydroxyacetone phosphate.
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