A three-state prediction of single point mutations on protein stability changes

Background: A basic question of protein structural studies is to which extent mutations affect the stability. This question may be addressed starting from sequence and/or from structure. In proteomics and genomics studies prediction of protein stability free energy change (G) upon single point mutation may also help the annotation process. The experimental G values are affected by uncertainty as measured by standard deviations. Most of the G values are nearly zero (about 32% of the G data set ranges from -0.5 to 0.5 kcal/mole) and both the value and sign of G may be either positive or negative for the same mutation blurring the relationship among mutations and expected G value. In order to overcome this problem we describe a new

• Type: Journal
• Year: 2008
• Where: BMCBI
• Authors: Emidio Capriotti, Piero Fariselli, Ivan Rossi, Rita Casadio
• Keywords: BMCBI 2008, Extent Mutations, Mutations, Stability Free Energy