Folding and aggregation of designed proteins.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 9789017.
- Also identified by PMC identifier 23658.
- No licence information is recorded for this record.
- Because redistribution is not established, this page shows the abstract only. Follow the links below for the full text.
Abstract
Protein aggregation is studied by following the simultaneous folding of two designed identical 20-letter amino acid chains within the framework of a lattice model and using Monte Carlo simulations. It is found that protein aggregation is determined by elementary structures (partially folded intermediates) controlled by local contacts among some of the most strongly interacting amino acids and formed at an early stage in the folding process.
Medical subject headings
- Peptides
- Protein Conformation
- Protein Folding
- Proteins