Conformation of the C-terminus of endothelin-1 in aqueous solution studied by Monte-Carlo simulation.
The conformation of the C-terminus of endothelin-1 in an aqueous solution has been analyzed by a Monte-Carlo simulation including the hydration energy term. The C-terminus may adopt multiple or flexible conformations in the solution, but the classification of the conformations shows that a comparably large number of conformers take a similar folding form in which the C-terminal chain is extended along the alpha-helix of the N-terminal core, and hydrophobic clusters are formed between the side groups of the C- and N-terminus. The aromatic ring of Trp21 is located at a certain distance from the two charged side groups of Asp8 and Glu10, and the functional groups of the key residues in the N-terminus are uncovered with the C-terminus tail.
Kuroda
M
M
Faculty of Pharmaceutical Sciences, Kyoto University, Japan.
Yamazaki
K
K
Taga
T
T
D000595:Amino Acid Sequence; D003198:Computer Simulation; D016232:Endothelins / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009010:Monte Carlo Method; D010446:Peptide Fragments / Q000737:chemistry*; D011487:Protein Conformation; D012996:Solutions; D013816:Thermodynamics; D014867:Water
D016232:Endothelins; D010446:Peptide Fragments; D012996:Solutions; D014867:Water