Role of solvent accessibility for aggregation-prone patches in protein folding.

ABSTRACT: The arrangement of amino acids in a protein sequence encodes its native folding. However, the same arrangement in aggregation-prone regions may cause misfolding as a result of local environmental stress. Under normal physiological conditions, such regions congregate in the protein's interior to avoid aggregation and attain the native fold. We have used solvent accessibility of aggregation patches (SAAP_p) to determine the packing of aggregation-prone residues. Our results showed that SAAP_p has low values for native crystal structures, consistent with protein folding as a mechanism to minimize the solvent accessibility of aggregation-prone residues. SAAP_p also shows an average correlation of 0.76 with the global distance test (GDT) score on CASP12 template-ba

SUBMITTER: Mishra A 

PROVIDER: S-EPMC6110721 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature