Detalles del Título
Detalles del Título

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Título Allostery: methods and protocolsLibros / Impreso - Libros
Autor(es) Fenton, Aron W. (Editor)
Publicación New York, NY : Humana Press, 2012
Descripción Física xviii, 439 p. : il. (algunas col.) 26 cm.
Idioma Inglés;
Series Methods in molecular biology (v. 796)
ISBN 1617793337
Clasificación(es) 572.643
Materia(s) Regulación alostérica; Proteínas alostéricas;
Nota(s) Incluye referencias bibliográficas e índice
CONTENIDO: Binding techniques to study the allosteric energy cycle -- Kinetic trapping of a key hemoglobin intermediate -- Allosteric coupling between transition metal binding sites in homooligomeric metal sensor proteins -- Studying the allosteric energy cycle by isothermal titration calorimetry -- Detecting ¿silent¿ allosteric coupling -- Using mutant cycle analysis to elucidate long-range functional coupling in allosteric receptors -- A review of methods used for identifying structural changes in a large protein complex -- Allosteric mechanisms of G protein-coupled receptor signaling: a structural perspective -- Dynamic light scattering to study allosteric regulation -- Dissecting the linkage between transcription factor self-assembly and site-specific DNA binding: the role of the analytical ultracentrifuge -- Fluorescence correlation spectroscopy and allostery: the case of GroEL --The morpheein model of allostery: evaluating proteins as potential morpheeins -- Combining NMR and molecular dynamics studies for insights into the allostery of small GTPase-protein interactions -- H/D-exchange study of an allosteric energy cycle -- Ensemble properties of network rigidity reveal allosteric mechanism -- An in vivo approach to isolating allosteric pathways using hybrid multimeric proteins -- Mutations in the GABAA receptor that mimic the allosteric ligand, etomidate -- Allosteric regulation of human liver pyruvate kinase by peptides that mimic the ated/dephosphorylated N-terminus -- In silico screening approaches for lead generation: identification of novel allosteric modulators of human-erythrocyte pyruvate kinase -- Identification of allosteric-activating drug leads for human liver pyruvate kinase -- A critical evaluation of correlated mutation algorithms and coevolution within allosteric mechanisms --The advantage of global fitting of data involving complex linked reactions -- Predicting binding sites by analyzing allosteric effects.
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CodBarras Localización Piso Signatura Estado Categoría
105430Biblioteca Universidad Icesi2572.643/A441DisponibleCol. General