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Science 15 February 1991:
Vol. 251. no. 4995, pp. 783 - 786
DOI: 10.1126/science.1990439
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Articles

Science, Vol 251, Issue 4995, 783-786
Copyright © 1991 by American Association for the Advancement of Science

articles

Determination of membrane protein structure by rotational resonance NMR: bacteriorhodopsin

F Creuzet, A McDermott, R Gebhard, K van der Hoef, MB Spijker-Assink, J Herzfeld, J Lugtenburg, MH Levitt, and RG Griffin

Francis Bitter National Magnet Laboratory, Massachusetts Institute of Technology, Cambridge 02139.

Rotationally resonant magnetization exchange, a new nuclear magnetic resonance (NMR) technique for measuring internuclear distances between like spins in solids, was used to determine the distance between the C-8 and C-18 carbons of retinal in two model compounds and in the membrane protein bacteriorhodopsin. Magnetization transfer between inequivalent spins with an isotropic shift separation, delta, is driven by magic angle spinning at a speed omega r that matches the rotational resonance condition delta = n omega r, where n is a small integer. The distances measured in this way for both the 6-s-cis- and 6-s-trans-retinoic acid model compounds agreed well with crystallographically known distances. In bacteriorhodopsin the exchange trajectory between C-8 and C-18 was in good agreement with the internuclear distance for a 6-s-trans configuration [4.2 angstroms (A)] and inconsistent with that for a 6-s-cis configuration (3.1 A). The results illustrate that rotational resonance can be used for structural studies in membrane proteins and in other situations where diffraction and solution NMR techniques yield limited information.


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