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• W2000449351 abstract "The solution conformation of acyl carrier protein from Escherichia coli (77 residues) has been determined on the basis of 423 interproton-distance restraints and 32 hydrogen-bonding restraints derived from NMR measurements. A total of nine structures were computed using a hybrid approach combining metric matrix distance geometry and dynamic simulated annealing. The polypeptide fold is well defined with an average backbone atomic root-mean-square difference of 0.20 ± 0.03 nm between the final nine converged structures and the mean structure obtained by averaging their coordinates. The principal structural motif is composed of three helices: 1 (residues 3–12), 2 (residues 37–47) and 4 (residues 65–75) which line a hydrophobic cavity. Helices 2 and 4 are approximately parallel to each other and anti-parallel at an angle of ≊ 150° to helix 1. The smaller helix 3 (residues 56–63) is at an angle of ≊ 100° to helix 4." @default.
• W2000449351 created "2016-06-24" @default.
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• W2000449351 date "1988-07-01" @default.
• W2000449351 modified "2023-09-25" @default.
• W2000449351 title "Three-dimensional structure of acyl carrier protein in solution determined by nuclear magnetic resonance and the combined use of dynamical simulated annealing and distance geometry" @default.
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• W2000449351 doi "https://doi.org/10.1111/j.1432-1033.1988.tb14159.x" @default.
• W2000449351 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/3402450" @default.
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