| Range |
1 – 2 kcal/mol
|
| Organism |
Unspecified |
| Reference |
Dill KA, Ozkan SB, Shell MS, Weikl TR. The protein folding problem. Annu Rev Biophys. 2008 37 :289-316. doi: 10.1146/annurev.biophys.37.092707.153558 p.291 right column 2nd paragraphPubMed ID18573083
|
| Primary Source |
[234] Wolfenden R. 2007. Experimental measures of amino acid hydrophobicity and the topology of transmembrane and globular proteins. J. Gen. Physiol. 129: 357–62 DOI: 10.1085/jgp.200709743PubMed ID17438117
|
| Comments |
P.291 right column 2nd paragraph: "There
is considerable evidence that hydrophobic interactions must play a major role in protein folding. (a) Proteins have hydrophobic cores, implying nonpolar amino acids are driven to be sequestered from water. (b) Model compound studies show 1–2 kcal/mol for transferring a hydrophobic side chain from water into oil-like media (primary source), and there are many of them." |
| Entered by |
Uri M |
| ID |
114428 |