Use of a Single Glycine Residue to Determine the Tilt and Orientation of a Transmembrane Helix. A New Structural Label for Infrared Spectroscopy
- 1 December 2000
- journal article
- Published by Elsevier in Biophysical Journal
- Vol. 79 (6) , 3139-3143
- https://doi.org/10.1016/s0006-3495(00)76547-7
Abstract
No abstract availableKeywords
This publication has 11 references indexed in Scilit:
- Structure of the Influenza C Virus CM2 Protein Transmembrane Domain Obtained by Site-specific Infrared Dichroism and Global Molecular Dynamics SearchingPublished by Elsevier ,2000
- vpu Transmembrane Peptide Structure Obtained by Site-Specific Fourier Transform Infrared Dichroism and Global Molecular Dynamics SearchingBiophysical Journal, 1999
- Experimentally based orientational refinement of membrane protein models: a structure for the Influenza A M2 H + channel 1 1Edited by G. von HeijneJournal of Molecular Biology, 1999
- Crystallography & NMR System: A New Software Suite for Macromolecular Structure DeterminationActa Crystallographica Section D-Biological Crystallography, 1998
- Transmembrane four-helix bundle of influenza A M2 protein channel: structural implications from helix tilt and orientationBiophysical Journal, 1997
- Site-Directed Dichroism As a Method for Obtaining Rotational and Orientational Constraints for Oriented PolymersJournal of the American Chemical Society, 1997
- Examination of the secondary structure of proteins by deconvolved FTIR spectraBiopolymers, 1986
- Vibrational analysis of peptides, polypeptides, and proteins. XV. Crystalline polyglycine IIBiopolymers, 1982
- Fourier Self-Deconvolution: A Method for Resolving Intrinsically Overlapped BandsApplied Spectroscopy, 1981
- Infrared spectra of isotopic polyglycinesBiopolymers, 1966