The allosteric modulation of thyroxine-binding globulin affinity is entropy driven

Background Thyroxine-binding globulin (TBG) is a non-inhibitory member of the serpin family of proteins whose main structural element is the reactive center loop (RCL), that, upon cleavage by proteases, is inserted into the protein core adopting a β-strand conformation (stressed to relaxed transitio...

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Guardado en:
Detalles Bibliográficos
Publicado: 2013
Materias:
Allostery
Conformational entropy
Generalized Born surface analysis
Molecular dynamics
Serpin family
Thyroxine-binding globulin
proteinase
thyroxine
thyroxine binding globulin
allosterism
article
binding affinity
binding site
complex formation
conformational transition
controlled study
entropy
enzyme activity
hydrogen bond
molecular dynamics
priority journal
protein binding
protein conformation
protein interaction
protein localization
protein secondary structure
protein stability
protein structure
reaction time
reactive center loop
structure analysis
Allosteric Regulation
Binding Sites
Crystallography, X-Ray
Entropy
Humans
Protein Structure, Secondary
Thyroxine
Thyroxine-Binding Globulin
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03044165_v1830_n6_p3570_Petruk
http://hdl.handle.net/20.500.12110/paper_03044165_v1830_n6_p3570_Petruk
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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