approach of examining separated parts of the structure – seeing the whole channel, including the
transmembrane region, is an extraordinarily informative event!
To place the problems in perspective, Jean-Luc Popot explores basic principles of membrane
architecture, from which point of view he develops the progressive insights of decades of advances in
membrane protein solubilization, leading to an extensive treatment of the amphiphilic polymers as the
most recent technology. In the text, a progressive set of issues are examined through the lens of the
enabling technologies used: protein solubilization, purification, folding, and expression; followed by
different methods that can be used: optical spectroscopy, NMR, crystallography, mass spectrometry,
and electron microscopy; and then followed by practical uses for solubilized membrane proteins:
surface immobilization and vaccines. Along the way, one is educated in the fundamental thinking that
guides the applications, so that a reader will both appreciate the established possibilities and perhaps
create new ones.
September 2017
Donald M. Engelman
References
Deisenhofer, J., Epp, O., Miki, K., Huber, R., Michel, H. (1984) X-ray structure analysis of a membrane protein complex.
Electron density map at 3 Å resolution and a model of the chromophores of the photosynthetic reaction center from
Rhodopseudomonas viridis. J. Mol. Biol. 180:385–398.
Henderson, R., Unwin, P.N.T. (1975) Three-dimensional model of purple membrane obtained by electron microscopy.
Nature 257:28–32.
Fig. 1 Structures of membrane proteins as imagined in 1972. The conceptualization lacks the insights on
secondary structure that followed soon afterward when electron microscopy evidence for transmembrane
α-helices was obtained in 1975 (Henderson and Unwin 1975), and, later, a detailed X-ray crystallography
structural model for the photosynthetic reaction center was elucidated in 1984 (Deisenhofer et al. 1984).
Still later, crystallographic evidence for the β-barrel structural theme emerged in 1990 (Weiss et al. 1990)
(Figure reproduced with permission from Singer and Nicolson 1972, # 1972 American Association for
the Advancement of Science).
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