Biology – Quantitative Biology – Genomics
Scientific paper
2009-12-28
PNAS 107(12) 5405-5410 (2010)
Biology
Quantitative Biology
Genomics
Scientific paper
10.1073/pnas.1001705107
Recognition of pathogens relies on families of proteins showing great diversity. Here we construct maximum entropy models of the sequence repertoire, building on recent experiments that provide a nearly exhaustive sampling of the IgM sequences in zebrafish. These models are based solely on pairwise correlations between residue positions, but correctly capture the higher order statistical properties of the repertoire. Exploiting the interpretation of these models as statistical physics problems, we make several predictions for the collective properties of the sequence ensemble: the distribution of sequences obeys Zipf's law, the repertoire decomposes into several clusters, and there is a massive restriction of diversity due to the correlations. These predictions are completely inconsistent with models in which amino acid substitutions are made independently at each site, and are in good agreement with the data. Our results suggest that antibody diversity is not limited by the sequences encoded in the genome, and may reflect rapid adaptation to antigenic challenges. This approach should be applicable to the study of the global properties of other protein families.
Bialek William
Callan Curtis G. Jr.
Mora Thierry
Walczak Aleksandra
No associations
LandOfFree
Maximum entropy models for antibody diversity 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 Maximum entropy models for antibody diversity, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Maximum entropy models for antibody diversity will most certainly appreciate the feedback.
Profile ID: LFWR-SCP-O-91925