Ab initio protein structure prediction: the necessary presence of external force field as it is delivered by Hsp40 chaperone.

ABSTRACT:

Background

The aqueous environment directs the protein folding process towards the generation of micelle-type structures, which results in the exposure of hydrophilic residues on the surface (polarity) and the concentration of hydrophobic residues in the center (hydrophobic core). Obtaining a structure without a hydrophobic core requires a different type of external force field than those generated by a water. The examples are membrane proteins, where the distribution of hydrophobicity is opposite to that of water-soluble proteins. Apart from these two extreme examples, the process of protein folding can be directed by chaperones, resulting in a structure devoid of a hydrophobic core.

Results

The current work presents such example: DnaJ Hsp40 in complex with alkaline phospha

SUBMITTER: Roterman I 

PROVIDER: S-EPMC10629080 | biostudies-literature | 2023 Nov

REPOSITORIES: biostudies-literature