Evolutionary Origin of a Secondary Structure: π-Helices as Cryptic but Widespread Insertional Variations of α-Helices That Enhance Protein Functionality
- 26 November 2010
- journal article
- Published by Elsevier BV in Journal of Molecular Biology
- Vol. 404 (2), 232-246
- https://doi.org/10.1016/j.jmb.2010.09.034
Abstract
No abstract availableKeywords
This publication has 43 references indexed in Scilit:
- In the light of directed evolution: Pathways of adaptive protein evolutionProceedings of the National Academy of Sciences of the United States of America, 2009
- On the occurrence of linear groups in proteinsProtein Science, 2009
- A Mycobacterium tuberculosis ligand-binding Mn/Fe protein reveals a new cofactor in a remodeled R2-protein scaffoldProceedings of the National Academy of Sciences of the United States of America, 2009
- Structural consequences of effector protein complex formation in a diiron hydroxylaseProceedings of the National Academy of Sciences of the United States of America, 2008
- Searching protein structure databases with DaliLite v.3Bioinformatics, 2008
- Mechanistic approaches to the study of evolution: the functional synthesisNature Reviews Genetics, 2007
- The Protein Data BankNucleic Acids Research, 2000
- CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choiceNucleic Acids Research, 1994
- The rapid generation of mutation data matrices from protein sequencesBioinformatics, 1992
- Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical featuresPeptide Science, 1983