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Refined structure of melittin bound to perdeuterated dodeclylphoscholine micelles as studied by 2D‐NMR and distance geometry calculation
Author(s) -
Ikura Teikichi,
Gō Nobuhiro,
Inagaki Fuyuhiko
Publication year - 1991
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340090202
Subject(s) - melittin , chemistry , hydrogen bond , crystallography , bent molecular geometry , micelle , geometry , distortion (music) , molecular physics , molecule , physics , mathematics , peptide , aqueous solution , amplifier , biochemistry , optoelectronics , organic chemistry , cmos
In our previous paper we reported the conformation of melittin bound to perdeuterated dodecylphosphocholine micelles as studied by 1 H NMR experiment and distance geometry calculation. No hydrogen bonds were taken into consideration explicitly in the calculation. However, mostly α‐helical conformations were obtained as results of the calculation even with no explicitly assumed hydrogen bonds. In the present paper we refined the distance geometry calculation by incorporating hydrogen bonds suggested by the previous calculation. As a result, we obtained the conformation of melittin, which was consistent with both NMR data and the additional hydrogen bonding data. The α‐helical rod in the refined conformation also has a kink at Thr‐11 and Gly‐12, but its bent angle is now a bit narrowly distributed in 135° × 15°. In the present study another distortion at Trp‐19 and IIe‐20 becomes conspicuous. The average root‐mean‐square displacement of atoms is now much smaller and is 1.5 Å for all backbone atoms. In the present paper side chain conformations are also analyzed.