✦ LIBER ✦

Structure and orientation of Apo B-100 peptides into a lipid bilayer

✍ Scribed by Laurence Lins; Robert Brasseur; Maryvonne Rosseneu; Chao -Yuh Yang; Doris A. Sparrow; James T. Sparrow; Antonio M. Gotto; Jean -Marie Ruysschaert

Publisher: Springer
Year: 1994
Tongue: English
Weight: 844 KB
Volume: 13
Category: Article
ISSN: 1573-4943
DOI: 10.1007/bf01891995

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

The structure and orientation of class-A

The structure and orientation of class-A amphipathic peptides on a phospholipid bilayer surface

✍ Andrew H. A. Clayton; W. H. Sawyer 📂 Article 📅 1999 🏛 Springer 🌐 English ⚖ 95 KB

Dynamics and orientation of transmembran

Dynamics and orientation of transmembrane peptide from bacteriorhodopsin incorporated into lipid bilayer as revealed by solid state 31P and 13C NMR spectroscopy

✍ Shigeki Kimura; Akira Naito; Satoru Tuzi; Hazime Saitô 📂 Article 📅 2001 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 185 KB 👁 2 views

Solid-state NMR analysis of the orientat

Solid-state NMR analysis of the orientation and dynamics of epigallocatechin gallate, a green tea polyphenol, incorporated into lipid bilayers

✍ Katsuko Kajiya; Shigenori Kumazawa; Akira Naito; Tsutomu Nakayama 📂 Article 📅 2008 🏛 John Wiley and Sons 🌐 English ⚖ 139 KB

## Abstract Catechins are the principle polyphenolic compounds in green tea; the four major compounds identified are epicatechin (EC), epigallocatechin (EGC), epicatechin gallate (ECg) and epigallocatechin gallate (EGCg). Tea catechins tend to attach externally to their targets, such as viral envel

Secondary structure and distribution of

Secondary structure and distribution of fusogenic LV-peptides in lipid membranes

✍ J. Ollesch; B. C. Poschner; J. Nikolaus; M. W. Hofmann; A. Herrmann; K. Gerwert; 📂 Article 📅 2007 🏛 Springer 🌐 English ⚖ 508 KB

Influence of thionin on the structure of

Influence of thionin on the structure of a bilayer and on the intermembrane exchange of lipid material

✍ S. O. Kolusheva; B. A. Salakhutdinov; T. F. Aripov; L. P. Vernon 📂 Article 📅 1994 🏛 Springer 🌐 English ⚖ 300 KB

Structural comparison in solution of a n

Structural comparison in solution of a native and retro peptide derived from the third helix of Staphylococcus aureus protein A, domain B: retro peptides, a useful tool for the discrimination of helix stabilization factors dependent on the peptide chain orientation

✍ Thomas Haack; Yolanda M. Sánchez; María-José González; Ernest Giralt 📂 Article 📅 1997 🏛 John Wiley and Sons 🌐 English ⚖ 515 KB

A peptide fragment corresponding to the third helix of Staphylococcus Aureus protein A, domain B, was chosen to study the effect of the main-chain direction upon secondary structure formation and stability, applying the retro-enantio concept. For this purpose, two peptides consisting of the native (