scholarly article | Q13442814 |
P356 | DOI | 10.1002/1521-3773(20011217)40:24<4615::AID-ANIE4615>3.0.CO;2-H |
P698 | PubMed publication ID | 12404364 |
P50 | author | Martin Karplus | Q903471 |
P2093 | author name string | Aaron R. Dinner | |
P2860 | cites work | Protein Folding: A Perspective from Theory and Experiment. | Q54308010 |
The Key to Solving the Protein-Folding Problem Lies in an Accurate Description of the Denatured State Financial support from the Schweizerischer Nationalfonds (Project no. 21-50929.97) is gratefully acknowledged | Q73444388 | ||
Proteins with selected sequences fold into unique native conformation | Q74548631 | ||
The Key to Solving the Protein-Folding Problem Lies in an Accurate Description of the Denatured State | Q95804539 | ||
Understanding protein folding via free-energy surfaces from theory and experiment | Q28139374 | ||
How does a protein fold? | Q28299554 | ||
Theory for the folding and stability of globular proteins | Q28307969 | ||
The fast protein folding problem | Q33199237 | ||
Three key residues form a critical contact network in a protein folding transition state | Q33935381 | ||
Topology, stability, sequence, and length: defining the determinants of two-state protein folding kinetics | Q34031904 | ||
The Levinthal paradox: yesterday and today | Q34436691 | ||
Understanding beta-hairpin formation | Q35594815 | ||
Engineering of stable and fast-folding sequences of model proteins | Q36455467 | ||
The roles of stability and contact order in determining protein folding rates. | Q52069638 | ||
Use of a quantitative structure-property relationship to design larger model proteins that fold rapidly. | Q52134728 | ||
P433 | issue | 24 | |
P304 | page(s) | 4615-4616 | |
P577 | publication date | 2001-12-01 | |
P1433 | published in | Angewandte Chemie International Edition | Q62023953 |
P1476 | title | Comment on the Communication "The Key to Solving the Protein-Folding Problem Lies in an Accurate Description of the Denatured State" by van Gunsteren et al. We thank Eugene Shakhnovich (Harvard University) for pointing out the references on lattice polymer simulations and very helpful discussions. We also thank Wilfred van Gunsteren for comments on the manuscript. A.R.D. is a Burroughs Wellcome Fund Hitchings-Elion Postdoctoral Fellow. The work done at Harvard was supported in part by the National Institutes of Health | |
P478 | volume | 40 |
Q36572197 | Fast protein folding on downhill energy landscape |
Q34989900 | Is polyproline II a major backbone conformation in unfolded proteins? |
Q52946664 | Methinks it is like a folding curve. |
Q34034318 | Polyproline II structure in a sequence of seven alanine residues. |
Q58616243 | Reply |
Q34989923 | Unfolded state of peptides |
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