A systematic structural comparison of all solved small proteins deposited in PDB. The effect of disulfide bonds in protein fold.

ABSTRACT: Defensins are small proteins, usually ranging from 3 to 6 kDa, amphipathic, disulfide-rich, and with a small or even absent hydrophobic core. Since a hydrophobic core is generally found in globular proteins that fold in an aqueous solvent, the peculiar fold of defensins can challenge tertiary protein structure predictors. We performed a Protein Data Bank survey of small proteins (3-6 kDa) to understand the similarities of defensins with other small disulfide-rich proteins. We found no differences when we compared defensins with non-defensins regarding the proportion of apolar, polar and charged residues and their exposure to the solvent. Then we divided all small proteins (3-6 kDa) in the Protein Data Bank into two groups, one group with at least one disulfide bond (bonded, defensins inclu

SUBMITTER: Moreira MH 

PROVIDER: S-EPMC8712280 | biostudies-literature | 2021

REPOSITORIES: biostudies-literature