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- W248889751 abstract "Publisher Summary This chapter presents the experience with photosensitive reagents designed to label the lipid core of membranes. Interpretation of labeling patterns in terms of possible structural features is hampered by the facts that intrinsic reactivities of amino acid side chains toward a carbene are not comparable, that no data exist as to the precise distribution of reagent molecules within a lipid bilayer and that nothing is known about the existence of specific or nonspecific interactions between reagent and protein. It is necessary to develop different labeling strategies to ascertain conclusions drawn from one type of experiments and to obtain a view of increased structural resolution. One promising approach along this line is the labeling of a protein in different structural states. In the intact F1 F0 ATP synthase, subunit c forms an oligomer containing 10±1 copies per F0. In SDS, this complex dissociates to yield monomers of subunit c, a process which is likely to be accompanied by major structural changes and, hence, changes in the residues available at the protein surface." @default.
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- W248889751 date "1983-01-01" @default.
- W248889751 modified "2023-09-26" @default.
- W248889751 title "PHOTOACTIVATABLE REAGENTS IN PROBING THE PROTEIN-LIPID INTERFACE OF MEMBRANES" @default.
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- W248889751 doi "https://doi.org/10.1016/b978-0-444-80540-9.50014-5" @default.
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