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

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 is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1002/1521-3773(20011217)40:24<4615::AID-ANIE4615>3.0.CO;2-H
P698PubMed publication ID12404364

P50authorMartin KarplusQ903471
P2093author name stringAaron R. Dinner
P2860cites workProtein 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 acknowledgedQ73444388
Proteins with selected sequences fold into unique native conformationQ74548631
The Key to Solving the Protein-Folding Problem Lies in an Accurate Description of the Denatured StateQ95804539
Understanding protein folding via free-energy surfaces from theory and experimentQ28139374
How does a protein fold?Q28299554
Theory for the folding and stability of globular proteinsQ28307969
The fast protein folding problemQ33199237
Three key residues form a critical contact network in a protein folding transition stateQ33935381
Topology, stability, sequence, and length: defining the determinants of two-state protein folding kineticsQ34031904
The Levinthal paradox: yesterday and todayQ34436691
Understanding beta-hairpin formationQ35594815
Engineering of stable and fast-folding sequences of model proteinsQ36455467
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
P433issue24
P304page(s)4615-4616
P577publication date2001-12-01
P1433published inAngewandte Chemie International EditionQ62023953
P1476titleComment 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
P478volume40

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cites work (P2860)
Q36572197Fast protein folding on downhill energy landscape
Q34989900Is polyproline II a major backbone conformation in unfolded proteins?
Q52946664Methinks it is like a folding curve.
Q34034318Polyproline II structure in a sequence of seven alanine residues.
Q58616243Reply
Q34989923Unfolded state of peptides

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