BCH 4024 Lecture Notes - Lecture 3: Alpha Helix, Imidazole, Covalent Bond

• School: University of Florida
• Department: Biochemistry and Molecular Biology
• Course: BCH 4024
• Professor: Daniel L Purich

Document Summary

Noncovalent interactions play key roles in living systems. While organic chemistry focuses on covalent bond rearrangements, living systems are highly dependent on both covalent bonds and noncovalent interactions. Unlike the considerable bond energies of single, double and triple bonds, the strengths of noncovalent binding interactions are tunable. Their weaker energies depend on many factors such as hydration, electrostatics, polarity, etc. Non covalent interactions are made and/or broken readily. Non covalent interactions determine protein structure and function; enzyme specificity; dna structure and function; membrane formation and stability; and nearly every other vital process in living systems. 4 basic types of interaction in biology. Individually weak, their overall effect can be very significant. Allows proteins and nucleic acids to fold and unfold on biology time-scale. H-bonds are easy to make & just as easy to break. Hydrogen -bonding per se is not a major driving force in protein folding. However, formation of extended h-bond networks act as structure-organizing elements.