Dissecting the disulphide-coupled folding pathway of bovine pancreatic trypsin inhibitor. Forming the first disulphide bonds in analogues of the reduced protein
- Autor
- DARBY, N. J1 ; CREIGHTON, T. E
[1] MRC, lab. molecular biology, Cambridge, United Kingdom - Fuente
Journal of molecular biology. 1993, Vol 232, Num 3, pp 873-896 ; ref : 1 p. 3/4
- CODEN
- JMOBAK
- ISSN
- 0022-2836
- Campo Científico
- Biochemistry, molecular biology, biophysics; Cell biology, histology; Biotechnology; Genetics
- Editor
- Elsevier, Oxford
- País de la publicación
- United Kingdom
- Tipo de documento
- Article
- Idioma
- English
- Palabra clave (fr)
- Bovin Cinétique Conformation In vitro Inhibiteur enzyme Intermédiaire réaction Liaison disulfure Repliement Trypsin Artiodactyla Enzyme Mammalia Ungulata Vertebrata
- Palabra clave (in)
- Bovine Kinetics Conformation In vitro Enzyme inhibitor Reaction intermediate Disulfide bond Refolding Trypsin Artiodactyla Enzyme Mammalia Ungulata Vertebrata
- Palabra clave (es)
- Bovino Cinética Conformación In vitro Inhibidor enzima Intermediario reacción Enlace disulfuro Repliegue Trypsin Artiodactyla Enzima Mammalia Ungulata Vertebrata
- Clasificación
- Pascal
- 002 Biological and medical sciences / 002A Fundamental and applied biological sciences. Psychology / 002A03 Molecular biophysics / 002A03G Structure in molecular biology / 002A03G01 Tridimensional structure
- Disciplina
- Molecular biophysics
- Procedencia
- Inist-CNRS
- Base de datos
- PASCAL
- Identificador INIST
- 4881004
Sauf mention contraire ci-dessus, le contenu de cette notice bibliographique peut être utilisé dans le cadre d’une licence CC BY 4.0 Inist-CNRS / Unless otherwise stated above, the content of this bibliographic record may be used under a CC BY 4.0 licence by Inist-CNRS / A menos que se haya señalado antes, el contenido de este registro bibliográfico puede ser utilizado al amparo de una licencia CC BY 4.0 Inist-CNRS
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DOI
10.1006/jmbi.1993.1437 
https://dx.doi.org/10.1006/jmbi.1993.1437
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