Proteins and peptides are digested with anhydrous hydrazine and the free amino acids, released from their carboxyl termini, are analyzed by reverse-phase chromatography as phenylthiocarbamyl (PTC) derivatives. Most of the potentially interfering hydrazides are removed due to the insolubility of thei
Determination of the Conformation of the Human VDAC1 N-Terminal Peptide, a Protein Moiety Essential for the Functional Properties of the Pore
✍ Scribed by Vito De Pinto; Flora Tomasello; Angela Messina; Francesca Guarino; Roland Benz; Diego La Mendola; Antonio Magrì; Danilo Milardi; Giuseppe Pappalardo
- Publisher
- John Wiley and Sons
- Year
- 2007
- Tongue
- English
- Weight
- 576 KB
- Volume
- 8
- Category
- Article
- ISSN
- 1439-4227
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
The 15 N-labeled C-terminal functional domain of the bacteriophage P22 scaffolding protein was expressed and purified. The NMR chemical-shift assignments of this functional domain were determined. An analysis of the chemical shift indices for the ˛-protons indicates that the N-terminal half of this
## Abstract Antigenicity in mice of a recombinant polypeptide including the complete amino acid sequence of mature human immunodeficiency virus type 1 p24 protein was studied by induction of monoclonal antibodies (MAbs). A panel of nine recloned hybridomas secreting MAbs with anti‐p24 reactivity wa
The free N-terminal 30-kDa domain of the fibronectin subunit chains had previously been shown to mediate binding of soluble fibrin to phagocytic cells. In order to demonstrate whether the fragment is available in plasma in a suitable concentration, an indirect immunoassay procedure for its quantitat
## Abstract The recently described human HSP22 belongs to the superfamily of small heat‐shock proteins containing a conservative α‐crystallin domain. HSP22 seems to be involved in regulation of cell proliferation, cardiac hypertrophy, apoptosis, and carcinogenesis, and expression of point mutants o