Ontology highlight
ABSTRACT:
SUBMITTER: Melnik TN
PROVIDER: S-EPMC4043776 | biostudies-literature | 2014
REPOSITORIES: biostudies-literature
Melnik Tatiana N TN Majorina Maria A MA Larina Daria S DS Kashparov Ivan A IA Samatova Ekaterina N EN Glukhov Anatoly S AS Melnik Bogdan S BS
PloS one 20140603 6
At present it is unclear which interactions in proteins reveal the presence of intermediate states, their stability and formation rate. In this study, we have investigated the effect of substitutions of hydrophobic amino acid residues in the hydrophobic core of protein and on its surface on a molten globule type intermediate state of apomyoglobin. It has been found that independent of their localization in protein, substitutions of hydrophobic amino acid residues do not affect the stability of t ...[more]