BCH 3125 Lecture Notes - Lecture 4: Peptide, Covalent Bond, Phospholipid

• School: University of Ottawa
• Department: Biochemistry
• Course: BCH 3125
• Professor: Corrie Da Costa

Document Summary

Problem set questions: true or false: most protein conformational changes involve breaking and reforming several covalent bonds along the polypeptide chain, fill in the blanks. Soluble proteins have mostly sidechains on the inside and mostly sidechains on the outside: the least restricted and angles are found in polypeptides in which class of secondary structure, right handed helix, sheet, loop left handed helix, fill in the blanks. In an helix, the of residue i hydrogen bonds with the of residue i + : why are helices in naturally occurring proteins almost always right handed, helices have what is known as a helical dipole moment. Although the bacteria have normal nucleic acids and proteins, the strain has an abnormal membrane. This extra thickness is entirely due to longer hydrophobic tails and not due to changes in the charged head groups of the phospholipids that comprise the membrane.