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|Title: ||Analysis of a complete DNA-protein affinity landscape|
|Authors: ||Rowe, William|
Wedge, David C.
Day, Philip J.R.
Kell, Douglas B.
|Keywords: ||Fitness landscapes|
|Issue Date: ||2010|
|Publisher: ||© Royal Society of Chemistry|
|Citation: ||ROWE, W., PLATT, M., WEDGE, D.C. ... et al, 2010. Analysis of a complete DNA-protein affinity landscape. Journal of the Royal Society Interface, 7 (44), pp.397-408.|
|Abstract: ||Properties of biological fitness landscapes are of interest to a wide sector of the life sciences,
from ecology to genetics to synthetic biology. For biomolecular fitness landscapes, the information
we currently possess comes primarily from two sources: sparse samples obtained from
directed evolution experiments; and more fine-grained but less authentic information from ‘in
silico’ models (such as NK-landscapes). Here we present the entire protein-binding profile of
all variants of a nucleic acid oligomer 10 bases in length, which we have obtained experimentally
by a series of highly parallel on-chip assays. The resulting complete landscape of
sequence-binding pairs, comprising more than one million binding measurements in duplicate,
has been analysed statistically using a number of metrics commonly applied to synthetic
landscapes. These metrics show that the landscape is rugged, with many local optima, and
that this arises from a combination of experimental variation and the natural structural
properties of the oligonucleotides.|
|Description: ||This article is closed access.|
|Version: ||Closed access|
|Publisher Link: ||http://dx.doi.org/10.1098/rsif.2009.0193|
|Appears in Collections:||Closed Access (Chemistry)|
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