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Membrane-based functions in the origin of cellular life
| Content Provider | NASA Technical Reports Server (NTRS) |
|---|---|
| Author | Wilson, Michael |
| Copyright Year | 1997 |
| Description | If peptides consist of nonpolar residues only, they become inserted into the nonpolar phase. As demonstrated by the example of the leucine undecamer, such peptides fold into an a-helix as they partition into the nonpolar medium. The folding proceeds through an intermediate, called the 310-helix, which remains in equilibrium with the a-helix. This process represents a simple, protobiologically relevant example of environmentally-mediated self-organization of biological molecules. Once in the nonpolar environment, the peptides can readily change their orientation with respect to the interface from parallel to perpendicular, especially in response to local electric fields. The ability of nonpolar peptides to modify both the structure and orientation with changing external conditions may have provided a simple mechanism of transmitting signals from the environment to the interior of a protocell. |
| File Size | 253870 |
| Page Count | 6 |
| File Format | |
| Alternate Webpage(s) | http://archive.org/details/NASA_NTRS_Archive_19980008786 |
| Archival Resource Key | ark:/13960/t0gv0j602 |
| Language | English |
| Publisher Date | 1997-01-01 |
| Access Restriction | Open |
| Subject Keyword | Residues Molecules Membranes Protobiology Cells Biology Peptides Biological Evolution Transmission Leucine Electric Fields Ntrs Nasa Technical Reports Server (ntrs) Nasa Technical Reports Server Aerodynamics Aircraft Aerospace Engineering Aerospace Aeronautic Space Science |
| Content Type | Text |
| Resource Type | Technical Report |
