The kingdom fungi contains many simple organisms like the one you see above. compare this fungus with the protist seen here, an algae called volvox. how do they differ in the way they obtain nutrients? a) both organisms are producers. volvox uses photosynthesis to get nutrients. the fungus uses chemosynthesis instead. b) both organisms are consumers. the volvox engulfs its food while the fungus absorbs food from the dead leaves using its hyphae. c) volvox is a producer and obtains nutrients through photosynthesis; the fungus is a consumer and is decomposing leaf litter in the forest. d) volvox gets nutrients through the process of photosynthesis. the fungus catches small insects under its cap and consumes the insects as food.

In familial hypercholesterolemia individuals homozygous for the allele causing the disorder completely lack receptors on liver cells that take up cholesterol from the blood stream. heterozygous have one-half the number of receptors while individuals homozygous for the normal allele are phenotypically normal. this is an example of a.epistasis b.complete dominance c. incomplete dominance d. codominance

Why do carbohydrate molecules function so well as fuel for the body?

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