Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 104, Issue 28, Pages 11627-11632Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0701393104
Keywords
protein designability; sequence capacity; structure stability; transitional sequences
Categories
Ask authors/readers for more resources
Sequence-structure relationships in proteins are highly asymmetric because many sequences fold into relatively few structures. What is the number of sequences that fold into a particular protein structure? Is it possible to switch between stable protein folds by point mutations? To address these questions, we compute a directed graph of sequences and structures of proteins, which is based on 2,060 experimentally determined protein shapes from the Protein Data Bank. The directed graph is highly connected at native energies with sinks that attract many sequences from other folds. The sinks are rich in beta-sheets. The number of sequences that transition between folds is significantly smaller than the number of sequences retained by their fold. The sequence flow into a particular protein shape from other proteins correlates with the number of sequences that matches this shape in empirically determined genomes. Properties of strongly connected components of the graph are correlated with protein length and secondary structure.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available