A remarkable emergent property of spontaneous (amino acid content) symmetry breaking

Biology – Quantitative Biology – Biomolecules

Scientific paper

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

Scientific paper

Learning how proteins fold will hardly have any impact in the way conventional -- active site centered -- drugs are designed. On the other hand, this knowledge is proving instrumental in defining a new paradigm for the identification of drugs against any target protein: folding inhibition. Targeting folding renders drugs less prone to elicit spontaneous genetic mutations which in many cases, notably in connection with viruses like the Human Immunodeficiency Virus (HIV), can block therapeutic action. From the progress which has taken place during the last years in the understanding of the becoming of a protein, and how to read from the corresponding sequences the associated three-dimensional, biologically active, native structure, the idea of non-conventional (folding) inhibitors and thus of leads to eventual drugs to fight disease, arguably, without creating resistance, emerges as a distinct possibility.

No associations

LandOfFree

Say what you really think

Search LandOfFree.com for scientists and scientific papers. Rate them and share your experience with other people.

Rating

A remarkable emergent property of spontaneous (amino acid content) symmetry breaking does not yet have a rating. At this time, there are no reviews or comments for this scientific paper.

If you have personal experience with A remarkable emergent property of spontaneous (amino acid content) symmetry breaking, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and A remarkable emergent property of spontaneous (amino acid content) symmetry breaking will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFWR-SCP-O-30600

  Search
All data on this website is collected from public sources. Our data reflects the most accurate information available at the time of publication.