Sandbox 14: Difference between revisions

<scene name='Sandbox_14/Trypsin/1'>Trypsin</scene> is a serine protease responsible for the hydrolysis of proteins. This process is biologically applicable in the process of digestion. Unlike other studied proteins such as αLytic Protease and Streptomyces griseus SGPB trypsin exists in a thermodynamically stable state and is inactiavated faster. Trypsin requires no pro region, like its counterparts αLP and SGPB, or its zymogen to fold. It was found that typsin had the same unfolding rate as αLP and SGPB therefore Truhlar et al have postulated that this succeptibility of trypsin to inactivation is due to the fact that trypsin is less optimized in suppressing unfolded state. This feature of trypsin is howver an evolutionary advantage since unlike αLP and SGPB which are extracellular, trypsin is released inside the gut of mammals and therefore has more of a need to be in its inactivated state.  Trypsin, like other serine proteases, is very specific in its reaction. It cleaves at peptide bonds located after residues with positive side chains, namely, arginine and lysine.