Substantial increase of protein stability by multiple disulphide bonds
- Author
- MATSUMURA, M1 ; SIGNOR, G; MATTHEWS, B. W
[1] Univ. Oregon, inst. molecular biology, Eugene OR 97403, United States - Source
Nature (London). 1989, Vol 342, Num 6247, pp 291-293 ; ref : 28 ref
- CODEN
- NATUAS
- ISSN
- 0028-0836
- Scientific domain
- Multidisciplinary
- Publisher
- Nature Publishing, London
- Publication country
- United Kingdom
- Document type
- Article
- Language
- English
- Keyword (fr)
- Bactériophage T4 Dénaturation renaturation Dénaturation thermique Enzyme Expression génique Liaison disulfure Lysozyme Mutagenèse dirigée Protéine Repliement Stabilité structurale Structure moléculaire Structure primaire Bactériophage Virus
- Keyword (en)
- Phage T4 Denaturation renaturation Thermal denaturation Enzyme Gene expression Disulfide bond Lysozyme Site directed mutagenesis Proteins Folding Structure stability Molecular structure Primary structure Phage Virus
- Keyword (es)
- Phage T4 Desnaturalización renaturalización Desnaturalización térmica Enzima Expresión genética Enlace disulfuro Lysozyme Mutagénesis dirigida Proteina Repliegue Estabilidad estructural Estructura molecular Estructura primaria Phage Virus
- Classification
- Pascal
- 002 Biological and medical sciences / 002A Fundamental and applied biological sciences. Psychology / 002A03 Molecular biophysics / 002A03G Structure in molecular biology / 002A03G04 Supramolecular structure
- Discipline
- Molecular biophysics
- Origin
- Inist-CNRS
- Database
- PASCAL
- INIST identifier
- 6687496
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
10.1038/342291a0 
https://dx.doi.org/10.1038/342291a0
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