Modelling biomolecules
H. Grant Guy, Richards W. Graham · Computational Chemistry · 1995
This chapter focuses on methods for modelling protein structures. In many circumstances it is now possible to make a reasonable prediction of the structure of a protein from its sequence. Multiple sequence data also allow the identification of the most likely mutations at particular positions across a family of homologous proteins. Extension of this information to include different structural classes provides excellent tools to approach the inverse folding problem. Once a sequence of unknown structure has been matched with a known structure, homology modelling methods can be used to effect the transformation of one structure into the other. Theoretical investigations of enzyme mechanisms are now also a possibility. Such methods are proving to be useful in understanding the molecular basis of enzyme activity.