Role of salt bridges in the dimer interface of 14-3-3Î¶ in dimer dynamics, N-terminal &#945;-helical order, and molecular chaperone activity.

Woodcock, Joanna M; Goodwin, Katy L; Sandow, Jarrod J; Coolen, Carl; Perugini, Matthew A; Webb, Andrew I; Pitson, Stuart M; Lopez, Angel F; Carver, John A

Role of salt bridges in the dimer interface of 14-3-3Î¶ in dimer dynamics, N-terminal α-helical order, and molecular chaperone activity.

Woodcock, Joanna M; Goodwin, Katy L; Sandow, Jarrod J; Coolen, Carl; Perugini, Matthew A; Webb, Andrew I; Pitson, Stuart M; Lopez, Angel F; Carver, John A.

Afiliação

Woodcock JM; Centre for Cancer Biology, University of South Australia and SA Pathology, Adelaide, South Australia 5000. Electronic address: Joanna.Woodcock@health.sa.gov.au.
Goodwin KL; School of Physical Sciences, University of Adelaide, Adelaide, South Australia 5005.
Sandow JJ; Division of Systems Biology and Personalised Medicine, Walter and Eliza Hall Institute of Medical Research, Parkville, Victoria 3052; Department of Medical Biology, University of Melbourne, Parkville, Victoria 3052.
Coolen C; Centre for Cancer Biology, University of South Australia and SA Pathology, Adelaide, South Australia 5000.
Perugini MA; Department of Biochemistry and Genetics, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, Victoria 3086.
Webb AI; Division of Systems Biology and Personalised Medicine, Walter and Eliza Hall Institute of Medical Research, Parkville, Victoria 3052; Department of Medical Biology, University of Melbourne, Parkville, Victoria 3052.
Pitson SM; Centre for Cancer Biology, University of South Australia and SA Pathology, Adelaide, South Australia 5000.
Lopez AF; Centre for Cancer Biology, University of South Australia and SA Pathology, Adelaide, South Australia 5000.
Carver JA; Research School of Chemistry, Australian National University, Acton, Australian Capital Territory 2601, Australia.

J Biol Chem ; 293(1): 89-99, 2018 01 05.

Article em En | MEDLINE | ID: mdl-29109150

Assuntos

Proteínas 14-3-3/química; Chaperonas Moleculares/química; Proteínas 14-3-3/genética; Proteínas 14-3-3/metabolismo; Sequência de Aminoácidos; Substituição de Aminoácidos; Humanos; Modelos Moleculares; Chaperonas Moleculares/genética; Chaperonas Moleculares/metabolismo; Mutação Puntual; Agregados Proteicos; Conformação Proteica em alfa-Hélice; Multimerização Proteica; Estabilidade Proteica; Sais/química; Sais/metabolismo; Alinhamento de Sequência

Palavras-chave

14-3-3 protein; analytical ultracentrifugation; dimer interface; dimerization; hydrogen-deuterium exchange; molecular chaperone; protein conformation; protein disorder; salt bridge

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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Chaperonas Moleculares / Proteínas 14-3-3 Tipo de estudo: Prognostic_studies Limite: Humans Idioma: En Ano de publicação: 2018 Tipo de documento: Article

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