NDLI: Predicting Protein Conformational Disorder and Disordered Binding Sites

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Predicting Protein Conformational Disorder and Disordered Binding Sites

Content Provider	Hyper Articles en Ligne (HAL)
Author	Tamburrini, Ketty Pesce, Giulia Nilsson, Juliet Gondelaud, Frank Kajava, Andrey Berrin, Jean-Guy Longhi, Sonia
Abstract	In the last two decades it has become increasingly evident that a large number of proteins adopt either a fully or a partially disordered conformation. Intrinsically disordered proteins are ubiquitous proteins that fulfill essential biological functions while lacking a stable 3D structure. Their conformational heterogeneity is encoded by the amino acid sequence, thereby allowing intrinsically disordered proteins or regions to be recognized based on their sequence properties. The identification of disordered regions facilitates the functional annotation of proteins and is instrumental for delineating boundaries of protein domains amenable to crystallization. This chapter focuses on the methods currently employed for predicting protein disorder and identifying intrinsically disordered binding sites.
Related Links	https://hal.science/hal-03834097/file/Chapter%20on%20disorder%20predictors%20310521%20%28S%20Longhi%29.pdf
DOI	10.1007/978-1-0716-2095-3_4
Volume Number	2449
Language	English
Publisher	HAL CCSD Springer US
Publisher Date	2022-05-05
Access Restriction	Open
Subject Keyword	intrinsically disordered binding sites intrinsic disorder intrinsically disordered proteins induced folding disorder databases and metaservers intrinsically disordered regions prediction methods and tools Life Sciences [q-bio]
Content Type	Text
Resource Type	Chapter
Subject	Biochemistry, Genetics and Molecular Biology

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