The membrane-binding properties of a class A amphipathic peptide
โ Scribed by H. Mozsolits; T.-H. Lee; A.H.A. Clayton; W.H. Sawyer; M.-I. Aguilar
- Publisher
- Springer
- Year
- 2004
- Tongue
- English
- Weight
- 402 KB
- Volume
- 33
- Category
- Article
- ISSN
- 1432-1017
No coin nor oath required. For personal study only.
๐ SIMILAR VOLUMES
## Calcium ions act as modulators of many fundamental processes in eukaryotic cells. Although these processes apparently involve initial interactions between calcium ions and cell membranes, the identity of the putative membrane Caz+binding proteins has until recently been obscure. This article de
A thermodynamic approach is proposed to quantitatively analyze the binding isotherms of peptides to model membranes as a function of one adjustable parameter, the actual peptide charge in solution z(p)+. The main features of this approach are a theoretical expression for the partition coefficient ca
he allele-specific peptidebinding motifs of major histocompatibility complex (MHC) proteins, originally discovered by pool sequencing of MHC class I-bound peptides 1 , provide a biochemical basis for the phenomenon of MHC restriction of T-cell responses. However, the analysis of class II peptide mot