The colicin E1 channel polypeptide was shown to be organized anisotropically in membranes by solid-state NMR analysis of samples of uniformly 15N-labeled protein in oriented planar phospholipid bilayers. The 190 residue C-terminal colicin E1 channel domain is the largest polypeptide to have been characterized by 15N solid-state NMR spectroscopy in oriented membrane bilayers. The 15N-NMR spectra of the colicin E1 show that: (1) the structure and dynamics are independent of anionic lipid content in both oriented and unoriented samples; (2) assuming the secondary structure of the polypeptide is helical, there are both trans-membrane and in-plane helical segments; (3) trans-membrane helices account for approximately 20-25\% of the channel polypeptide, which is equivalent to 38-48 residues of the 190-residue polypeptide. The results of the two-dimensional PISEMA spectrum are interpreted in terms of a single trans-membrane helical hairpin inserted into the bilayer from each channel molecule. These data are also consistent with this helical hairpin being derived from the 38-residue hydrophobic segment near the C-terminus of the colicin E1 channel polypeptide.
%0 Journal Article
%1 kim_solid-state_1998
%A Kim, Y
%A Valentine, K
%A Opella, S J
%A Schendel, S L
%A Cramer, W A
%D 1998
%J Protein Sci.
%K Acid Amino Data,Phospholipids Proteins,Molecular Resonance Sequence Sequence,Colicins,Lipid Spectroscopy,Membrane bilayers,Magnetic
%N 2
%P 342--348
%R 10.1002/pro.5560070214
%T Solid-state \NMR\ studies of the membrane-bound closed state of the colicin \E\1 channel domain in lipid bilayers
%V 7
%X The colicin E1 channel polypeptide was shown to be organized anisotropically in membranes by solid-state NMR analysis of samples of uniformly 15N-labeled protein in oriented planar phospholipid bilayers. The 190 residue C-terminal colicin E1 channel domain is the largest polypeptide to have been characterized by 15N solid-state NMR spectroscopy in oriented membrane bilayers. The 15N-NMR spectra of the colicin E1 show that: (1) the structure and dynamics are independent of anionic lipid content in both oriented and unoriented samples; (2) assuming the secondary structure of the polypeptide is helical, there are both trans-membrane and in-plane helical segments; (3) trans-membrane helices account for approximately 20-25\% of the channel polypeptide, which is equivalent to 38-48 residues of the 190-residue polypeptide. The results of the two-dimensional PISEMA spectrum are interpreted in terms of a single trans-membrane helical hairpin inserted into the bilayer from each channel molecule. These data are also consistent with this helical hairpin being derived from the 38-residue hydrophobic segment near the C-terminus of the colicin E1 channel polypeptide.
@article{kim_solid-state_1998,
abstract = {The colicin E1 channel polypeptide was shown to be organized anisotropically in membranes by solid-state NMR analysis of samples of uniformly 15N-labeled protein in oriented planar phospholipid bilayers. The 190 residue C-terminal colicin E1 channel domain is the largest polypeptide to have been characterized by 15N solid-state NMR spectroscopy in oriented membrane bilayers. The 15N-NMR spectra of the colicin E1 show that: (1) the structure and dynamics are independent of anionic lipid content in both oriented and unoriented samples; (2) assuming the secondary structure of the polypeptide is helical, there are both trans-membrane and in-plane helical segments; (3) trans-membrane helices account for approximately 20-25{\%} of the channel polypeptide, which is equivalent to 38-48 residues of the 190-residue polypeptide. The results of the two-dimensional PISEMA spectrum are interpreted in terms of a single trans-membrane helical hairpin inserted into the bilayer from each channel molecule. These data are also consistent with this helical hairpin being derived from the 38-residue hydrophobic segment near the C-terminus of the colicin E1 channel polypeptide.},
added-at = {2017-03-14T02:48:56.000+0100},
author = {Kim, Y and Valentine, K and Opella, S J and Schendel, S L and Cramer, W A},
biburl = {https://www.bibsonomy.org/bibtex/2f88265ce41d32360bdbd94363346e2eb/nmrresource},
doi = {10.1002/pro.5560070214},
interhash = {65b7e9ab0d53ed62878f79b462b1a8e7},
intrahash = {f88265ce41d32360bdbd94363346e2eb},
issn = {0961-8368},
journal = {Protein Sci.},
keywords = {Acid Amino Data,Phospholipids Proteins,Molecular Resonance Sequence Sequence,Colicins,Lipid Spectroscopy,Membrane bilayers,Magnetic},
month = feb,
number = 2,
pages = {342--348},
pmid = {9521110},
timestamp = {2017-03-14T02:49:21.000+0100},
title = {{Solid-state {\{}NMR{\}} studies of the membrane-bound closed state of the colicin {\{}E{\}}1 channel domain in lipid bilayers}},
volume = 7,
year = 1998
}