Physics – Condensed Matter – Statistical Mechanics
Scientific paper
2002-06-20
PNAS 99, 11163 (2002)
Physics
Condensed Matter
Statistical Mechanics
21 pages, 6 figures, to appear in PNAS
Scientific paper
10.1073/pnas.162105999
A typical protein structure is a compact packing of connected alpha-helices and/or beta-strands. We have developed a method for generating the ensemble of compact structures a given set of helices and strands can form. The method is tested on structures composed of four alpha-helices connected by short turns. All such natural four-helix bundles that are connected by short turns seen in nature are reproduced to closer than 3.6 Angstroms per residue within the ensemble. Since structures with no natural counterpart may be targets for ab initio structure design, the designability of each structure in the ensemble -- defined as the number of sequences with that structure as their lowest energy state -- is evaluated using a hydrophobic energy. For the case of four alpha-helices, a small set of highly designable structures emerges, most of which have an analog among the known four-helix fold families, however several novel packings and topologies are identified.
Emberly Eldon
Tang Changbing
Wingreen Ned
No associations
LandOfFree
Designability of alpha-helical Proteins does not yet have a rating. At this time, there are no reviews or comments for this scientific paper.
If you have personal experience with Designability of alpha-helical Proteins, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Designability of alpha-helical Proteins will most certainly appreciate the feedback.
Profile ID: LFWR-SCP-O-255601