Protein structure quality assessment based on the distance profiles of consecutive backbone Cα atoms.

ABSTRACT: Predicting the three dimensional native state structure of a protein from its primary sequence is an unsolved grand challenge in molecular biology. Two main computational approaches have evolved to obtain the structure from the protein sequence - ab initio/de novo methods and template-based modeling - both of which typically generate multiple possible native state structures. Model quality assessment programs (MQAP) validate these predicted structures in order to identify the correct native state structure. Here, we propose a MQAP for assessing the quality of protein structures based on the distances of consecutive Cα atoms. We hypothesize that the root-mean-square deviation of the distance of consecutive Cα (RDCC) atoms from the ideal value of 3.8 Å, derived from a statistical analysis of

SUBMITTER: Chakraborty S 

PROVIDER: S-EPMC3892923 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature