Mendel studied discrete, qualitative traits in peas. this organism him induce the rules of inheritance. his work dealt with simple dominant/recessive relationships between alleles. however, expression of many traits are not governed by a single gene, rather can involve multiple genes as well as additive effects. this kind of inheritance pattern is known as quantitative (see cogbooks -> genetic analysis of populations for more information). edward m east (1916) studied a continuously varying phenotype characteristic in nicotiana longiflora. he took pure-breeding lines of n. longiflora growing long corollas and crossed them with pure-breeding lines growing short corollas. after crossing these lines, f1 offspring had an intermediate length for corolla and had same variation level as in parents. but found a very different result for f2 and f3 than expected. discuss the reasons for this result and if it agrees/disagrees with mendel’s law. using obtained knowledge so far, what kind of cumulative effects would you add to this variation

Pick twenty foods and research the amount of total carbohydrates, sugars, and other carbohydrates in them. note: most food labels have this information. record your findings.

Here's one way to follow the scientific method. place the missing steps in the correct position in the process.

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