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...

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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
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Abstract 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.
AbstractList 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 acid 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.
Fifty years ago the Nobel Prize in chemistry was awarded to Max Perutz and John Kendrew for determining the structure of globular proteins. Since first viewing their structure of myoglobin, scientists have sought to understand protein folding. Dill and MacCallum (p. 1042) review the progress that has been made on three central questions: What is the code that relates sequence to structure? How do proteins fold so fast? Can protein structure be computationally predicted? While we have come some way toward answering these questions, new questions have been gene rated. It is no longer useful to talk about "solving the protein-folding problem"--protein folding has grown into a field of research where the next 50 years promise to be as exciting as the last. [PUBLICATION ABSTRACT] 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 acid 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. [PUBLICATION ABSTRACT]
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.
Fifty years ago the Nobel Prize in chemistry was awarded to Max Perutz and John Kendrew for determining the structure of globular proteins. Since first viewing their structure of myoglobin, scientists have sought to understand protein folding. Dill and MacCallum (p. 1042 ) review the progress that has been made on three central questions: What is the code that relates sequence to structure? How do proteins fold so fast? Can protein structure be computationally predicted? While we have come some way toward answering these questions, new questions have been gene rated. It is no longer useful to talk about “solving the protein-folding problem”—protein folding has grown into a field of research where the next 50 years promise to be as exciting as the last. 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 acid 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.
Author Dill, Ken A.
MacCallum, Justin L.
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https://www.ncbi.nlm.nih.gov/pubmed/23180855$$D View this record in MEDLINE/PubMed
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Snippet 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...
Fifty years ago the Nobel Prize in chemistry was awarded to Max Perutz and John Kendrew for determining the structure of globular proteins. Since first viewing...
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SubjectTerms Algorithms
Alzheimers disease
Amino Acid Sequence
Amino acids
Analytical, structural and metabolic biochemistry
Biological and medical sciences
Caspase 9 - chemistry
Computer Simulation
Fundamental and applied biological sciences. Psychology
History
Modeling
Models, Chemical
Molecular and cellular biology
Molecules
Organic Chemistry
Parkinson disease
Personal computers
Pharmaceutical Preparations - chemistry
Polymers
Protein Conformation
Protein Folding
Proteins - chemistry
Proteostasis deficiencies
REVIEW
Title The Protein-Folding Problem, 50 Years On
URI https://www.jstor.org/stable/41703986
https://www.ncbi.nlm.nih.gov/pubmed/23180855
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