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Peptides at Membrane Surfaces and their Role in the Origin of LifeAll ancestors of contemporary cells (protocells) had to transport ions and organic matter across membranous walls, capture and utilize energy and transduce environmental signals. In modern organisms, all these functions are preformed by membrane proteins. We make the parsimonious assumption that in the protobiological milieu the same functions were carried out by their simple analogs - peptides. This, however, required that simple peptides could self-organize into ordered, functional structures. In a series of detailed, molecular-level computer simulations we demonstrated how this is possible. One example is the peptide (LSLLLSL)3 which forms a trameric bundle capable of transporting protons across membranes. Another example is the transmembrane pore of the influenza M2 protein. This aggregate of four identical alpha-helices, each built of 25 amino acids, forms an efficient and selective voltage-gated proton channel. Our simulations explain the gating mechanism in this channel. The channel can be re-engineered into a simple proton pump.
Document ID
20030001118
Acquisition Source
Ames Research Center
Document Type
Conference Paper
Authors
Pohorille, Andrew
(NASA Ames Research Center Moffett Field, CA United States)
Wilson, Michael A.
(NASA Ames Research Center Moffett Field, CA United States)
DeVincenzi, D.
Date Acquired
August 21, 2013
Publication Date
January 1, 2002
Subject Category
Life Sciences (General)
Meeting Information
Meeting: American Chemical Society Meeting
Location: Boston, MA
Country: United States
Start Date: August 18, 2002
End Date: August 22, 2002
Sponsors: American Chemical Society
Funding Number(s)
PROJECT: RTOP 344-38-22-06
Distribution Limits
Public
Copyright
Work of the US Gov. Public Use Permitted.

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