Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 357908
Title Conformation of a peptide encompassing the proton translocation channel of vacuolar H+-ATPase
Author(s) Vos, W.L.; Vermeer, L.S.; Hemminga, M.A.
Source Biophysical Journal 92 (2007). - ISSN 0006-3495 - p. 138 - 146.
Department(s) Biophysics
Publication type Refereed Article in a scientific journal
Publication year 2007
Keyword(s) yeast v-atpase - molecular-dynamics simulations - electron-spin-resonance - coiled-coils - alpha-helix - pi-helix - protein - subunit - domain - receptor
Abstract The structural properties of a crucial transmembrane helix for proton translocation in vacuolar ATPase are studied using double site-directed spin-labeling combined with electron spin resonance (ESR) (or electron paramagnetic resonance) and circular dichroism spectroscopy in sodium dodecyl sulfate micelles. For this purpose, we use a synthetic peptide derived from transmembrane helix 7 of subunit a from the yeast Saccharomyces cerevisiae vacuolar proton-translocating ATPase that contains two natural cysteine residues suitable for spin-labeling. The interspin distance is calculated using a second-moment analysis of the methanethiosulfonate spin-label ESR spectra at 150 K. Molecular dynamics simulation is used to study the effect of the side-chain dynamics and backbone dynamics on the interspin distance. Based on the combined results from ESR, circular dichroism, and molecular dynamics simulation we conclude that the peptide forms a dynamic -helix. We discuss this finding in the light of current models for proton translocation. A novel role for a buried charged residue (H729) is proposed.
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