The diagram below shows the interrelationship between two processes. Within which organelle do Process A and Process B occur? WILL MARK BRAINLIESTTT

A) Both occur within the mitochondria.
B) Both occur within the chloroplast.
C) Process A occurs within the chloroplast and Process B occurs within the mitochondria.
D) Process A occurs within the mitochondria and Process B occurs within the chloroplast.

Y’all i need answers plss people are saying me and my brother look alike although we’re two different ages. one year apart i’m a girl, btw i’m thinking we could be fraternal twins idk my parents and my friends think we look alike

Over the past 60 years, many amphibian species have experienced significant population declines and some species have become extinct. scientists suspected that local human activities such as the destruction of wetlands, regional pollution, and deforestation were the main reasons for these losses. however, research over the past 20 years reveals significant amphibian population declines in protected areas of the world, such as nature preserves and parks. these global declines suggest widespread problems including increased ultraviolet radiation, acid rain, and disease. in switzerland, for example, 14 of the 20 native amphibian species are threatened with extinction. chytridiomycosis is a fungal disease first identified in 1998 as a cause of massive amphibian deaths. in some severely impacted populations, a few individuals have survived, perhaps because of some natural resistance. if these resistant individuals continue to survive and prosper, new resistant populations might emerge. this would be an example of the founder effect artificial selection genetic drift natural selection sexual selection

Match the descriptions / definitions with the term they best describe 1. three dimensional relationship of the different polypeptide chains in a multisubunit protein or protein complex 2. common folding pattern in proteins in which a linear sequence of amino acids folds into a right-handed coil stabilized by internal hydrogen-bonding between polypeptide backbone atoms. 3. the amino acid sequence of a protein 4. a region on the surface of a protein that can interact with another molecule through noncovalent bonding. 5. three-dimensional arrangement of alpha-helices and beta-sheets within a single polypeptide, typically stabilized by a variety of noncovalent bonds, including ionic and hydrogen bonds, and nonpolar interactions / hydrophobic force. 6. the chain of repeating carbon and nitrogen atoms, linked by peptide bonds, in a protein. 7. common structural motif in proteins in which different sections of the polypeptide chain run alongside each other and are joined together by hydrogen bonding between atoms of the polypeptide backbone. 8. portion of a polypeptide chain that has a discrete tertiary structure of its own and can often fold independently of the rest of the chain 9. regular local folding patterns in a protein, including alpha-helix and beta-sheet a. primary structure b. beta-sheet c. protein d. coiled-coil e. polypeptide backbone f. secondary structure g. side chain h. tertiary structure i. binding site j. alpha-helix k. quaternary structure l. protein domain