Structural Characterization of Highly Flexible Proteins by Small-Angle Scattering.
Adv Exp Med Biol
; 1009: 107-129, 2017.
Article
em En
| MEDLINE
| ID: mdl-29218556
ABSTRACT
Intrinsically Disordered Proteins (IDPs) are fundamental actors of biological processes. Their inherent plasticity facilitates very specialized tasks in cell regulation and signalling, and their malfunction is linked to severe pathologies. Understanding the functional role of disorder requires the structural characterization of IDPs and the complexes they form. Small-angle Scattering of X-rays (SAXS) and Neutrons (SANS) have notably contributed to this structural understanding. In this review we summarize the most relevant developments in the field of SAS studies of disordered proteins. Emphasis is given to ensemble methods and how SAS data can be combined with computational approaches or other biophysical information such as NMR. The unique capabilities of SAS enable its application to extremely challenging disordered systems such as low-complexity regions, amyloidogenic proteins and transient biomolecular complexes. This reinforces the fundamental role of SAS in the structural and dynamic characterization of this elusive family of proteins.
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Texto completo:
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Base de dados:
MEDLINE
Assunto principal:
Modelos Moleculares
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Espalhamento a Baixo Ângulo
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Proteínas Amiloidogênicas
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Proteínas Intrinsicamente Desordenadas
Limite:
Humans
Idioma:
En
Ano de publicação:
2017
Tipo de documento:
Article