WATER ACCESSIBILITY TO TRYPTOPHAN RESIDUES IN HORSE APOMYOGLOBIN

Citation
A. Haouz et al., WATER ACCESSIBILITY TO TRYPTOPHAN RESIDUES IN HORSE APOMYOGLOBIN, Chemical physics letters, 279(1-2), 1997, pp. 79-84
Citations number
28
Categorie Soggetti
Physics, Atomic, Molecular & Chemical
Journal title
ISSN journal
00092614
Volume
279
Issue
1-2
Year of publication
1997
Pages
79 - 84
Database
ISI
SICI code
0009-2614(1997)279:1-2<79:WATTRI>2.0.ZU;2-R
Abstract
Water molecules are generally considered not to reach the buried hydro phobic center of proteins. A study on tryptophan residues embedded in the A, G, H helices cluster from horse apomyoglobin shows that water m olecules can access these residues. It is suggested that the arrival o f water at the buried residues could result from the protein's specifi c flexibility, which is itself regulated by the solvation state of the protein surface. (C) 1997 Elsevier Science B.V.