Ineed these qustions ! plz 1.why do organisms do meiosis? a. to make more skin and muscle cells in their bodies b. to make gametes (sperm or eggs) c. just for fun! d. all of the above 2.what happens during metaphase i? a. tetrads line up down the middle of the cell. b. chromatin condenses to form visible chromosomes. c. homologous chromosomes separate and move toward opposite ends of the cell. d. all of the above 3. which of the following are true? a. cytokinesis is the division of the cytoplasm to form two separate cells. b. cytokinesis may occur at the same time as telophase i. c. the two new cells produced at the end of telophase i and cytokinesis are hapoid. d. all of the above 4.how is prophase ii different than prophase i? a. tetrads do not form in prophase ii. b. the nucleus does not go away during prophase ii. c. there are no hromosomes during prophase ii. d. all of the above 5. what happens during telophase ii? a. each newly forming cell gets a nucleus b. chromosomes uncoil to form chromatin. c. 4 haploid gametes are being formed. d. all of the above. 6. what are the final results after telophase ii and cytokinesis are finished? a. 4 diploid gametes b. 2 diploid gametes c. 4 haploid gametes d. 2 haploid gametes 7. which of the following are true statements? a. dna replicates during interphase. b. chromatin is made of dna. c. genes are found on dna. d. all of the above.

What is one benefit of a non renewable resource, such as natural gas? a. generates large amounts of electricity b. less expensive c. produces pollution d. will run out eventually

Which class of molecules contains the amino group, nh2 (a) sugars (b) water (c) proteins (d) hydrocarbons

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