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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.
Author(s) -
Dinner Aaron R.,
Karplus Martin
Publication year - 2001
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/1521-3773(20011217)40:24<4615::aid-anie4615>3.0.co;2-h
Subject(s) - protein folding , scaling , key (lock) , folding (dsp implementation) , conformational isomerism , scaling law , statistical physics , computer science , state (computer science) , mathematical economics , mathematics , physics , algorithm , engineering , quantum mechanics , geometry , computer security , nuclear magnetic resonance , molecule , electrical engineering
Which scaling connects the number of conformers of a protein with the number of residues? The authors both explore this question and van Gunsteren et al. produce additional arguments to those in their original paper. Although the authors do not agree on the “scaling law”, they both acknowledge the importance of finding the correct answer as it has a great influence on the chance of simulating protein folding with reasonably good models.