Secondary structure of acyl carrier protein as derived from two-dimensional proton NMR spectroscopy
- 23 September 1986
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 25 (19) , 5766-5774
- https://doi.org/10.1021/bi00367a063
Abstract
Sequence-specific assignments of 1H NMR resonances were obtained for the backbone protons in acyl carrier protein (ACP) from Escherichia coli, a protein of 77 residues. The observations, in the NOESY spectra, of 1H.sbd.1H sequential and medium-range connectives indicate the presence of three or four .alpha.-helical segments joined by short sequences of mixed conformations. The observations are used to refine a secondary structure model previously proposed on the basis of a Chou-Fasman algorithm [Rock, C.O., and Cronan, J.E., Jr. (1979) J. Biol. Chem. 254, 9778-9785].This publication has 18 references indexed in Scilit:
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