Abstract:
:Molecular dynamics simulation, with backbone constraints for 20 ps of equilibration and simulation, of a repeating polypeptide segment, Gln-Pro-His-Gln-Pro-Leu-Gln-Pro-His-Gln-Pro-Leu-Gln-Pro-Met-(Gln-Pro-Leu )4, constituting residues 112-138 of bovine amelolgenin, a 19.35 kD hydrophobic protein, are discussed. It is generally believed that the above polypeptide segment is important for the interaction of amelogenin with Ca++ ions, which occurs in the early phases of enamel mineralization. An energetically stable structure of the above polypeptide with recurrent beta-turns is observed and contains a pore of approximately 1 A radius along the helical that can accommodate an unhydrated Ca++ ion. The length of the polypeptide possesses correct dimensions to span a bilayer. The proposed structure is unique among known polypeptide and protein structures.
journal_name
Biopolymersjournal_title
Biopolymersauthors
Renugopalakrishnan V,Pattabiraman N,Prabhakaran M,Strawich E,Glimcher MJdoi
10.1002/bip.360280130subject
Has Abstractpub_date
1989-01-01 00:00:00pages
297-303issue
1eissn
0006-3525issn
1097-0282journal_volume
28pub_type
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