Thousands of proteins likely to have long disordered regions

Autor:	P, Romero, Z, Obradovic, C R, Kissinger, J E, Villafranca, E, Garner, S, Guilliot, A K, Dunker
Rok vydání:	1998
Předmět:	Internet Structure-Activity Relationship Databases Factual Sequence Homology Amino Acid Calcineurin Animals Humans Proteins Reproducibility of Results False Positive Reactions Amino Acid Sequence Sequence Alignment Software
Zdroj:	Pacific Symposium on Biocomputing. Pacific Symposium on Biocomputing.
ISSN:	2335-6928
Popis:	Neural network predictors of protein disorder using primary sequence information were developed and applied to the Swiss Protein Database. More than 15,000 proteins were predicted to contain disordered regions of at least 40 consecutive amino acids, with more than 1,000 having especially high scores indicating disorder. These results support proposals that consideration of structure-activity relationships in proteins need to be broadened to include unfolded or disordered protein.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::7c6a8b4ded8feff1539685045fdc4e77 https://pubmed.ncbi.nlm.nih.gov/9697202 Zobrazit plný text záznamu