The Protein-Folding Problem, 50 Years On

The protein-folding problem was first posed about one half-century ago. The term refers to three broad questions: (i) What is the physical code by which an amino add sequence dictates a protein's native structure? (ii) How can proteins fold so fast? (iii) Can we devise a computer algorithm to p...

Full description

Saved in:
Bibliographic Details
Published inScience (American Association for the Advancement of Science) Vol. 338; no. 6110; pp. 1042 - 1046
Main Authors Dill, Ken A., MacCallum, Justin L.
Format Journal Article
LanguageEnglish
Published Washington, DC American Association for the Advancement of Science 23.11.2012
The American Association for the Advancement of Science
Subjects
Online AccessGet full text

Cover

Loading…
More Information
Summary:The protein-folding problem was first posed about one half-century ago. The term refers to three broad questions: (i) What is the physical code by which an amino add sequence dictates a protein's native structure? (ii) How can proteins fold so fast? (iii) Can we devise a computer algorithm to predict protein structures from their sequences? We review progress on these problems. In a few cases, computer simulations of the physical forces in chemically detailed models have now achieved the accurate folding of small proteins. We have learned that proteins fold rapidly because random thermal motions cause conformational changes leading energetically downhill toward the native structure, a principle that is captured in funnel-shaped energy landscapes. And thanks in part to the large Protein Data Bank of known structures, predicting protein structures is now far more successful than was thought possible in the early days. What began as three questions of basic science one half-century ago has now grown into the full-fledged research field of protein physical science.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-3
content type line 23
ObjectType-Review-1
ISSN:0036-8075
1095-9203
DOI:10.1126/science.1219021