Crucial stages of protein folding through a solvable model: Predicting target sites for enzyme‐inhibiting drugs

An exactly solvable model based on the topology of a protein native state is applied to identify bottlenecks and key sites for the folding of human immunodeficiency virus type 1 (HIV‐1) protease. The predicted sites are found to correlate well with clinical data on resistance to Food and Drug Administration‐approved drugs. It has been observed that the effects of drug therapy are to induce multiple mutations on the protease. The sites where such mutations occur correlate well with those involved in folding bottlenecks identified through the deterministic procedure proposed in this study. The high statistical significance of the observed correlations suggests that the approach may be promisingly used in conjunction with traditional techniques to identify candidate locations for drug attacks.

• Publication year

  2002

• Venue

  Protein Science

• Publication date

  2002-08-01

• Fields of study

  Biology, Medicine, Physics, Chemistry

• Identifiers
  DOI 10.1110/ps.3360102arXiv cond-mat/0209325PMID 12142442PMCID PMC2373687
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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