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NMR structural studies of peptides and proteins in membranes

Miscellaneous:

Abstract

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 19 refs., 9 figs.
Authors:
Opella, S J [1] 
  1. Pennsylvania Univ., Philadelphia, PA (United States). Dept. of Chemistry
Publication Date:
Dec 31, 1993
Product Type:
Miscellaneous
Report Number:
CONF-9305442-
Reference Number:
SCA: 400101; PA: AIX-29:044606; EDB-98:088425; SN: 98001996591
Resource Relation:
Conference: 4. meeting of the nuclear magnetic resonance users, 4. Encontro de usuarios de ressonancia magnetica nuclear, Angra dos Reis (Brazil), 11-15 May 1993; Other Information: DN: 19 refs., 9 figs.; PBD: 1993; Related Information: Is Part Of Proceedings of the 4. Meeting of the nuclear magnetic resonance users; PB: 465 p.; Anais do 4. Encontro de usuarios de ressonancia magnetica nuclear
Subject:
40 CHEMISTRY; CELL MEMBRANES; CELL WALL; MOLECULAR STRUCTURE; NUCLEAR MAGNETIC RESONANCE; PROTEIN STRUCTURE; PROTEINS; QUALITATIVE CHEMICAL ANALYSIS; STRUCTURAL CHEMICAL ANALYSIS
OSTI ID:
636227
Research Organizations:
Associacao de Usuarios de Ressonancia Magnetica Nuclear, Rio de Janeiro, RJ (Brazil)
Country of Origin:
Brazil
Language:
English
Other Identifying Numbers:
TRN: BR98B0207044606
Availability:
Available from the library of the Brazilian Nuclear Energy Commission, Rio de Janeiro
Submitting Site:
BRN
Size:
pp. 75-102
Announcement Date:

Miscellaneous:

Citation Formats

Opella, S J. NMR structural studies of peptides and proteins in membranes. Brazil: N. p., 1993. Web.
Opella, S J. NMR structural studies of peptides and proteins in membranes. Brazil.
Opella, S J. 1993. "NMR structural studies of peptides and proteins in membranes." Brazil.
@misc{etde_636227,
title = {NMR structural studies of peptides and proteins in membranes}
author = {Opella, S J}
abstractNote = {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 19 refs., 9 figs.}
place = {Brazil}
year = {1993}
month = {Dec}
}