Kloczkowski Andrzej, Jernigan Robert L
Baker Center for Bioinformatics and Biological Statistics, Iowa State University, 123 Office and Lab Bldg., Ames 50011-3020, USA.
J Biomol Struct Dyn. 2002 Dec;20(3):323-5. doi: 10.1080/07391102.2002.10506849.
We show that loops of close contacts involving hydrophobic residues are important in protein folding. Contrary to Berezovsky Berezovsky and Trifonov (J Biomol Struct Dyn 20, 5-6, 2002) the loops important in protein folding usually are much larger in size than 23-31 residues, being instead comparable to the size of the protein for single domain proteins. Additionally what is important are not single loop contacts, but a highly interconnected network of such loop contacts, which provides extra stability to a protein fold and which leads to their conservation in evolution.
