Folding of Polypeptide Chains in Proteins: A Proposed Mechanism for Folding

AUTOR(ES)

Lewis, Peter N.

RESUMO

A mechanism is proposed for the folding of protein chains. On the basis of short-range interactions, certain aminoacid sequences have a high propensity to be, say, α-helical. However, these short helical (or other ordered) regions can be stabilized only by long-range interactions arising from the proximity of two such ordered regions. These regions are brought near each other by the directing influence of certain other aminoacid sequences that have a high probability of forming β-bends or variants thereof, also on the basis of short-range interactions. An analysis is made of the tendency of various amino acids to occur in β-bends, and it is possible to predict the regions of a chain in which a β-bend will occur with a high degree of reliability.

Documentos Relacionados

• The folding mechanism of larger model proteins: role of native structure.
• NORMAL COUNTERPARTS TO BENCE-JONES PROTEINS: FREE L POLYPEPTIDE CHAINS OF HUMAN γ-GLOBULIN*
• A proposed mechanism for the self-splicing of proteins.
• Proposed mechanism for stability of proteins to evolutionary mutations
• The Flory isolated-pair hypothesis is not valid for polypeptide chains: Implications for protein folding