Published 1993
| Version v1
Miscellaneous
NMR structural studies of peptides and proteins in membranes
Description
The use of NMR methodology in structural studies is described as applicable to larger proteins, considering that the majority of membrane proteins is constructed from a limited repertoire of structural and dynamic elements. The membrane associated domains of these proteins are made up of long hydrophobic membrane spanning helices, shorter amphipathic bridging helices in the plane of the bilayer, connecting loops with varying degrees of mobility, and mobile N- and C- terminal sections. NMR studies have been successful in identifying all of these elements and their orientations relative to each other and the membrane bilayer
Additional details
Additional titles
- Original title (English)
- Anais do 4. Encontro de usuarios de ressonancia magnetica nuclear
Publishing Information
- Imprint Title
- Proceedings of the 4. Meeting of the nuclear magnetic resonance users
- Imprint Pagination
- 465 p.
- Journal Page Range
- p. 75-102
Conference
- Title
- 4. meeting of the nuclear magnetic resonance users
- Original Conference Title
- 4. Encontro de usuarios de ressonancia magnetica nuclear
- Dates
- 11-15 May 1993
- Place
- Angra dos Reis, RJ (Brazil)
INIS
- Country of Publication
- Brazil
- Country of Input or Organization
- Brazil
- INIS RN
- 29044606
- Subject category
- S37: INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY;
- Resource subtype / Literary indicator
- Conference, Non-conventional Literature
- Descriptors DEI
- CELL MEMBRANES; CELL WALL; MOLECULAR STRUCTURE; NUCLEAR MAGNETIC RESONANCE; PROTEIN STRUCTURE; PROTEINS; QUALITATIVE CHEMICAL ANALYSIS; STRUCTURAL CHEMICAL ANALYSIS
- Descriptors DEC
- CELL CONSTITUENTS; CHEMICAL ANALYSIS; MAGNETIC RESONANCE; MEMBRANES; ORGANIC COMPOUNDS; RESONANCE
Optional Information
- Notes
- 19 refs., 9 figs. Imprint:Anais do 4. Encontro de usuarios de ressonancia magnetica nuclear