We have created a SNP database that contains wildtype and SNP protein simulations.
Our aim is to facilitate analysis of SNP pathologies and how they relate to the
structure, stability, function, and dynamics of the protein. Our SNP database currently
contains approximately 200 single-point mutations and their counterpart wildtype
proteins. In total, 31 proteins are represented. A subset of these proteins and
their associated diseases are listed below in Table 1.
Our simulations have provided insights into the structural mechanisms behind the
protein destabilization of several SNP mutants. One common theme is the structural
disruption of a protein at a location distant from the point of the SNP mutation.
The simulation of the V108M mutation in catechol O-methyltransferase, for example,
reveals a 16 Å separation between the amino acid substitution point and the structurally
disrupted enzyme active site [1, 2]. The crystal structures of this protein with
bound cofactor and substrate analog are very similar and do not show these large
differences . Other SNP simulations such as histamine N-methyltransferase ,
thiopurine S-methyltransferase , DJ-1 , and the DNA glycosylase/β-lyase hOgg1
 have also shown this long-range disruptive behavior.