Nicholas B. Last, Ph.D.

Protein Folding and Dynamics, Structural Biology

Andrew D. Miranker	grad student	2005-2012	Yale
(Membrane Poration by Islet Amyloid Polypeptide and the Common Mechanism Shared with Antimicrobial Peptide Magainin 2.)
Christopher Miller	post-doc	2012-2018	Brandeis

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Last NB, Stockbridge RB, Wilson AE, et al. (2018) A CLC-type F/H antiporter in ion-swapped conformations. Nature Structural & Molecular Biology
Last NB, Sun S, Pham MC, et al. (2017) Molecular determinants of permeation in a fluoride-specific ion channel. Elife. 6
Last NB, Kolmakova-Partensky L, Shane T, et al. (2016) Mechanistic signs of double-barreled structure in a fluoride ion channel. Elife. 5
Last NB, Miller C. (2015) Functional Monomerization of a ClC-Type Fluoride Transporter. Journal of Molecular Biology. 427: 3607-12
Last NB, Schlamadinger DE, Miranker AD. (2013) A common landscape for membrane-active peptides. Protein Science : a Publication of the Protein Society. 22: 870-82
Last NB, Miranker AD. (2013) Common mechanism unites membrane poration by amyloid and antimicrobial peptides. Proceedings of the National Academy of Sciences of the United States of America. 110: 6382-7
Last NB, Rhoades E, Miranker AD. (2011) Islet amyloid polypeptide demonstrates a persistent capacity to disrupt membrane integrity. Proceedings of the National Academy of Sciences of the United States of America. 108: 9460-5