BCH 4024 Lecture 6: L6

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

Document Summary

Maximizes the number of hydrophobic groups within the interior and giving great stability. Well defined diffusivity that is predictable on the basis of molecular weight, size and shape. Show spectroscopic evidence of a well folded structure. Arrange themselves into well-defined crystals that are suitable for. Intensive variable that is defined as mol substance bound per mol protein. Usually one binding site on each polypeptide chain. Defined as a micromol reaction product formed per minute per mg enzyme. Fully active proteins must fold on a biologically relevant timescale: Bacteria can double in number in as little as 18 min. ~2500 different proteins produced throughout a microorganism"s growth cycle. Proves that proteins must fold within minutes or less. Most small proteins fold spontaneously into a functionally active conformation. Estimated that 5% of all polypeptides emerged from ribosomes will fail to fold and or require assistance. So much that cells produce a set of foldases.