Sequence complexity of disordered protein
Top Cited Papers
- 2 November 2000
- journal article
- research article
- Published by Wiley in Proteins-Structure Function and Bioinformatics
Abstract
Intrinsic disorder refers to segments or to whole proteins that fail to self‐fold into fixed 3D structure, with such disorder sometimes existing in the native state. Here we report data on the relationships among intrinsic disorder, sequence complexity as measured by Shannon's entropy, and amino acid composition. Intrinsic disorder identified in protein crystal structures, and by nuclear magnetic resonance, circular dichroism, and prediction from amino acid sequence, all exhibit similar complexity distributions that are shifted to lower values compared to, but significantly overlapping with, the distribution for ordered proteins. Compared to sequences from ordered proteins, these variously characterized intrinsically disordered segments and proteins, and also a collection of low‐complexity sequences, typically have obviously higher levels of protein‐specific subsets of the following amino acids: R, K, E, P, and S, and lower levels of subsets of the following: C, W, Y, I, and V. The Swiss Protein database of sequences exhibits significantly higher amounts of both low‐complexity and predicted‐to‐be‐disordered segments as compared to a non‐redundant set of sequences from the Protein Data Bank, providing additional data that nature is richer in disordered and low‐complexity segments compared to the commonness of these features in the set of structurally characterized proteins. Proteins 2001;42:38–48.Keywords
This publication has 65 references indexed in Scilit:
- From protein structure to functionCurrent Opinion in Structural Biology, 1999
- Beyond complete genomes: from sequence to structure and functionCurrent Opinion in Structural Biology, 1998
- 4E Binding Proteins Inhibit the Translation Factor eIF4E without Folded StructureBiochemistry, 1998
- Probing protein structure using biochemical and biophysical methodsJournal of Chromatography A, 1997
- The C-terminal half of the anti-sigma factor, FlgM, becomes structured when bound to its target, σ28Nature Structural & Molecular Biology, 1997
- The recognition of protein structure and function from sequence: adding value to genome dataPhilosophical Transactions Of The Royal Society B-Biological Sciences, 1994
- Principles that Govern the Folding of Protein ChainsScience, 1973
- Application of a Theory of Enzyme Specificity to Protein SynthesisProceedings of the National Academy of Sciences of the United States of America, 1958
- On the Structure of Native, Denatured, and Coagulated ProteinsProceedings of the National Academy of Sciences, 1936
- Einfluss der Configuration auf die Wirkung der EnzymeEuropean Journal of Inorganic Chemistry, 1894