Transmembrane segments (TM) are important structural elements that often define the functional domain of membrane proteins.'.2 Structural studies of TM segments are thus becoming essential for understanding the structure/ function of membrane proteins, although their physical properties have often c
Conformations of Primary Amphipathic Carrier Peptides in Membrane Mimicking Environments †
✍ Scribed by Chaloin, Laurent; Vidal, Pierre; Heitz, Annie; Van Mau, Nicole; Méry, Jean; Divita, Gilles; Heitz, Frédéric
- Book ID
- 125896169
- Publisher
- American Chemical Society
- Year
- 1997
- Tongue
- English
- Weight
- 309 KB
- Volume
- 36
- Category
- Article
- ISSN
- 0006-2960
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
## Abstract The mechanism of membrane interaction by β‐sheet peptides is important to understand fundamental principles of folding of β‐barrel proteins and various β‐amyloid proteins. Here, we examined the conformational characteristics of a porin‐like channel forming (__x__S__x__G)~6~ peptide in s
Enkephalin represents one of the bioactive peptide molecules most extensively investigated both in solution and in the crystal state. Depending upon the environment chosen for such studies, three main conformational states were identified for this flexible, linear pentapeptide-i.e., an extended conf
## Abstract To identify rules for the design of efficient CPPs that can deliver therapeutic agents such as nucleic acids (DNAs, siRNAs) or proteins and PNAs into subcellular compartments, we compared the properties of several primary and secondary amphipathic CPPs. Studies performed with lipid mono