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Conformation of the C‐terminus of endothelin‐1 in aqueous solution studied by Monte‐Carlo simulation
Author(s) -
Kuroda Masataka,
Yamazaki Kazuto,
Taga Tooru
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)01217-2
Subject(s) - aqueous solution , c terminus , folding (dsp implementation) , monte carlo method , chemistry , n terminus , side chain , terminal (telecommunication) , conformational isomerism , crystallography , molecular dynamics , protein folding , stereochemistry , amino acid , computational chemistry , peptide sequence , molecule , computer science , biochemistry , mathematics , organic chemistry , telecommunications , statistics , electrical engineering , gene , engineering , polymer
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 α‐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 Trp 21 is located at a certain distance from the two charged side groups of Asp 8 and Glu 10 , and the functional groups of the key residues in the N‐terminus are uncovered with the C‐terminus tail.