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What role do bacteria play in the carbon cycle

In tossing one coin 10 times, what are your chances for tossing a head? a tail? 2. in tossing one coin 100 times, what are your chances for tossing a head? a tail? 3. in tossing one coin 200 times, what are your chances for tossing a head? a tail? deviation = ((absolute value of the difference between expected heads and observed heads) + (absolute value of the difference between expected tails and observed tails)) divided by total number of tosses. this value should always be positive. 4. what is the deviation for 10 tosses? 5. what is the deviation for the 100 tosses? 6. what is the deviation for 200 tosses? 7. how does increasing the total number of coin tosses from 10 to 100 affect the deviation? 8. how does increasing the total number of tosses from 100 to 200 affect the deviation? 9. what two important probability principles were established in this exercise? 10. the percent of occurrence is the obtained results divided by the total tosses and multiplied by 100%. toss the coins 100 times and record your results. calculate the percent occurrence for each combination. percent head-head occurrence: percent tail-tail occurrence: percent head-tail occurrence:

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