In vitro thermal denaturation experiments suggest that, because of the possibility of irreversible alterations, thermodynamic stability (i.e., a positive value for the unfolding Gibbs energy) does not guarantee that a protein will remain in the native state during a given timescale. Furthermore, irr
β¦ LIBER β¦
Thermal Stability: A Means to Assure Tertiary Structure in Therapeutic Proteins
β Scribed by Mike Cauchy; Sophie D'aoust; Brian Dawson; Harold Rode; Mary Alice Hefford
- Book ID
- 112237852
- Publisher
- Elsevier Science
- Year
- 2002
- Tongue
- English
- Weight
- 188 KB
- Volume
- 30
- Category
- Article
- ISSN
- 1045-1056
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
Lower kinetic limit to protein thermal s
β
Isabel M. Plaza del Pino; Beatriz Ibarra-Molero; Jose M. Sanchez-Ruiz
π
Article
π
2000
π
John Wiley and Sons
π
English
β 183 KB
π 1 views
Attenuated total reflection IR spectrosc
β
C. Vigano; L. Manciu; F. Buyse; E. Goormaghtigh; J.-M. Ruysschaert
π
Article
π
2000
π
Wiley (John Wiley & Sons)
π
English
β 119 KB
π 1 views
Attenuated total reflection IR spectrosc
β
I Martin; E Goormaghtigh; J.-M Ruysschaert
π
Article
π
2003
π
Elsevier Science
π
English
β 140 KB
Compositional and Structural Features Re
β
Francisco Miralles
π
Article
π
2011
π
Springer
π
English
β 633 KB
Adsorption of insulin with varying self-
β
Lene Jorgensen; Pernille Bennedsen; SΓΈren VrΓΈnning Hoffmann; Rasmus Linnemann Kr
π
Article
π
2011
π
Elsevier Science
π
English
β 537 KB
A novel mutation impairing the tertiary
β
Xiao-Qiao Li; Hong-Chen Cai; Shi-Yi Zhou; Ju-Hua Yang; Yi-Bo Xi; Xiao-Bo Gao; We
π
Article
π
2011
π
John Wiley and Sons
π
English
β 593 KB
Congenital cataract is one of the leading causes of human blindness. In this study, we identified a novel, heterozygous c.385G>T mutation in CRYGC that resulted in the substitution of a highly conserved glycine by cysteine at codon 129 (p.Gly129Cys) in a three-generation Chinese family with autosoma