The shape of the bacterial ribosome exit tunnel affects cotranslational protein folding.

Kudva, Renuka; Tian, Pengfei; Pardo-Avila, Fátima; Carroni, Marta; Best, Robert B; Bernstein, Harris D; von Heijne, Gunnar

Kudva, Renuka; Tian, Pengfei; Pardo-Avila, Fátima; Carroni, Marta; Best, Robert B; Bernstein, Harris D; von Heijne, Gunnar.

Afiliação

Kudva R; Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.
Tian P; Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, United States.
Pardo-Avila F; Department of Structural Biology, Stanford University, Stanford, United States.
Carroni M; Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.
Best RB; Science for Life Laboratory, Stockholm University, Solna, Sweden.
Bernstein HD; Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, United States.
von Heijne G; Genetics and Biochemistry Branch, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, United States.

Elife ; 72018 11 26.

Article em En | MEDLINE | ID: mdl-30475203

Assuntos

Escherichia coli/genética; Dobramento de Proteína; Ribossomos/genética; Escherichia coli/química; Simulação de Dinâmica Molecular; Biossíntese de Proteínas/genética; Domínios Proteicos/genética; Dedos de Zinco/genética

Palavras-chave

E. coli; arrest peptide; biochemistry; chemical biology; cotranslational; molecular biophysics; protein folding; ribosome; structural biology; uL23; uL24

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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Ribossomos / Dobramento de Proteína / Escherichia coli Idioma: En Ano de publicação: 2018 Tipo de documento: Article

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