Internal dynamics of the homotrimeric HIV-1 viral coat protein gp41 on multiple time scales.

Abstract

Always on the move: Solution NMR spectroscopy revealed a high degree of intrinsic mobility for the homotrimeric viral coat protein gp41: a prehairpin intermediate (left) may sample a range of relative orientations of the C-terminal and N-terminal heptad repeats, possibly in exchange with a low population of the late-fusion six-helical bundle (right; FP: fusion peptide, TM: transmembrane helix). As a service to our authors and readers, this journal provides supporting information supplied by the authors. Such materials are peer reviewed and may be re-organized for online delivery, but are not copy-edited or typeset. Technical support issues arising from supporting information (other than missing files) should be addressed to the authors. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.