NMR Characterization of Long-Range Contacts in Intrinsically Disordered Proteins from Paramagnetic Relaxation Enhancement in <sup>13</sup> C Direct-Detection Experiments.

Mateos, Borja; Konrat, Robert; Pierattelli, Roberta; Felli, Isabella C

NMR Characterization of Long-Range Contacts in Intrinsically Disordered Proteins from Paramagnetic Relaxation Enhancement in ¹³ C Direct-Detection Experiments.

Mateos, Borja; Konrat, Robert; Pierattelli, Roberta; Felli, Isabella C.

Afiliação

Mateos B; Department of Structural and Computational Biology, Max F. Perutz Laboratories, Vienna Biocenter Campus 5, 1030, Vienna, Austria.
Konrat R; Department of Structural and Computational Biology, Max F. Perutz Laboratories, Vienna Biocenter Campus 5, 1030, Vienna, Austria.
Pierattelli R; CERM and Department of Chemistry "Ugo Schiff", University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Florence, Italy.
Felli IC; CERM and Department of Chemistry "Ugo Schiff", University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Florence, Italy.

Chembiochem ; 20(3): 335-339, 2019 02 01.

Article em En | MEDLINE | ID: mdl-30407719

Assuntos

Proteínas Intrinsicamente Desordenadas/análise; Proteínas Intrinsicamente Desordenadas/química; Ressonância Magnética Nuclear Biomolecular; Isótopos de Carbono; Proteínas Intrinsicamente Desordenadas/metabolismo; Mutação; Osteopontina/química; Osteopontina/genética; Osteopontina/metabolismo

Palavras-chave

NMR spectroscopy; carbon; magnetic properties; proteins; structure elucidation

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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Ressonância Magnética Nuclear Biomolecular / Proteínas Intrinsicamente Desordenadas Idioma: En Ano de publicação: 2019 Tipo de documento: Article

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