A molecule of glycogen is formed by linking glucose molecules through this process. The separation of polymers into smaller units makes use of this process. This process does not involve breaking peptide bonds, but it does involve unfolding protein structure. The addition of water to break proteins into amino acids is an example of this process. Dehydration Synthesis Using acids to cook raw fish is an example of this process. This process removes water to link two or more amino acids. Denaturation Breaking DNA into nucleotides involves this process. The change to the color and consistency of an egg during cooking is an example of this process. Monomers are linked together through this process. Hydrolysis

The disulfide bond between two cysteine residues—     is a weak ion-induced dipole attraction.     is an ionic bond that is stable at physiological pH.     is a covalent bond formed by oxidation.     is a hydrogen bond between the two sulfhydryl groups.     is a special form of peptide bond.

Which of the following are NOT a level of biological structure?     macromolecular level     cellular/ organelle levels     tissue/ organ level     organismal level     all of the above     none of the above   Which of the following are steps in the biosynthesis of proteins can be regulated?     macromolecular level     cellular/ organelle levels     tissue/ organ level     organismal level     all of the above     none of the above.

When pharmacology researchers design drugs that must enter into cells in order to be effective, they often add functional groups to the drug to make it more likely to pass through the plasma membrane. The addition of which of the following functional groups would be most likely to increase the permeability of a drug across a membrane? Select an answer and submit. For keyboard navigation, use the up/down arrow keys to select an answer. a Amino. Carboxyl. Hydroxyl. d Methyl. e Phosphate.

Which of the following regarding disulfide bonds is/are true? Disulfide bonds are the most common intrachain covalent linkage in proteins Disulfide bond formation is critical for correct protein folding into the native conformation Disulfide bonds impart a large degree of stability to the secondary structure of proteins The intracellular environment is too oxidizing to allow disulfide bond formation A and D

During hydrogenation, cis double bonds are converted to trans double bonds.  In the lab, we compare three fats, each of which has fatty acid chains that are exactly the same length (number of carbons) and observe the following: Fat 1 contains only saturated fatty acids 16 carbons long, and has a melting point of 65 degrees C. Fat 2 contains only cis unsaturated fatty acids 16 carbons long, and has a melting point of 35 degrees C. Fat 3 contains only trans fatty acids 16 carbons long, and has a melting point of 65 degrees C. Both Fat 2 and Fat 3 contain fatty acids with a single double bond; fat 1 has no double bonds.  Why do Fat 3 and Fat 1 have more similar melting points than Fat 3 and Fat 2? Group of answer choices The number of hydrogen atoms in the fatty acids of fats 1 & 3 is higher, and having more hydrogen atoms raises the melting point of the fat. The fatty acids in fats 1 & 3 have a linear shape, so they pack tightly together and have lots of hydrophobic…