NDLI: Amide vibrations are delocalized across the hydrophobic interface of a transmembrane helix dimer

Content Provider	PubMed Central
Author	Fang, Chong Senes, Alessandro Cristian, Lidia Degrado, William F. Hochstrasser, Robin M.
Copyright Year	2006
Abstract	The tertiary interactions between amide-I vibrators on the separate helices of transmembrane helix dimers were probed by ultrafast 2D vibrational photon echo spectroscopy. The 2D IR approach proves to be a useful structural method for the study of membrane-bound structures. The 27-residue human erythrocyte protein Glycophorin A transmembrane peptide sequence: KKITLIIFG 79VMAGVIGTILLISWG 94IKK was labeled at G 79 and G 94 with 13C 16O or 13C 18O. The isotopomers and their 50:50 mixtures formed helical dimers in SDS micelles whose 2D IR spectra showed components from homodimers when both helices had either 13C 16O or 13C 18O substitution and a heterodimer when one had 13C 16O substitution and the other had 13C 18O substitution. The cross-peaks in the pure heterodimer 2D IR difference spectrum and the splitting of the homodimer peaks in the linear IR spectrum show that the amide-I mode is delocalized across a pair of helices. The excitation exchange coupling in the range 4.3–6.3 cm−1 arises from through-space interactions between amide units on different helices. The angle between the two Gly79 amide-I transition dipoles, estimated at 103° from linear IR spectroscopy and 110° from 2D IR spectroscopy, combined with the coupling led to a structural picture of the hydrophobic interface that is remarkably consistent with results from NMR on helix dimers. The helix crossing angle in SDS is estimated at 45°. Two-dimensional IR spectroscopy also sets limits on the range of geometrical parameters for the helix dimers from an analysis of the coupling constant distribution.
Related Links	http://dx.doi.org/10.1073/pnas.0608243103
Ending Page	16745
Page Count	6
Starting Page	16740
File Format	PDF
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	45
Volume Number	103
Language	English
Publisher	National Academy of Sciences
Publisher Date	2006-11-07
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Amide vibrations are delocalized across the hydrophobic interface of a transmembrane helix dimer.

A helix-to-coil transition at the ε-cut site in the transmembrane dimer of the amyloid precursor protein is required for proteolysis

Hydrophobic mismatch and sequence specificity compete when transmembrane helix-helix interactions are measured with the TOXCAT assay

Residue specific vibrational echoes yield 3-dimensional structures of a transmembrane helix dimer

Implications of threonine hydrogen bonding in the glycophorin A transmembrane helix dimer.

The Influence of Fatty Acids on the GpA Dimer Interface by Coarse-Grained Molecular Dynamics Simulation

Detergent Properties Influence the Stability of the Glycophorin A Transmembrane Helix Dimer in Lysophosphatidylcholine Micelles

Specificity in transmembrane helix–helix interactions can define a hierarchy of stability for sequence variants

On the thermodynamic stability of a charged arginine side chain in a transmembrane helix

Amide vibrations are delocalized across the hydrophobic interface of a transmembrane helix dimer

Similar Documents

Amide vibrations are delocalized across the hydrophobic interface of a transmembrane helix dimer.

A helix-to-coil transition at the ε-cut site in the transmembrane dimer of the amyloid precursor protein is required for proteolysis

Hydrophobic mismatch and sequence specificity compete when transmembrane helix-helix interactions are measured with the TOXCAT assay

Residue specific vibrational echoes yield 3-dimensional structures of a transmembrane helix dimer

Implications of threonine hydrogen bonding in the glycophorin A transmembrane helix dimer.

The Influence of Fatty Acids on the GpA Dimer Interface by Coarse-Grained Molecular Dynamics Simulation

Detergent Properties Influence the Stability of the Glycophorin A Transmembrane Helix Dimer in Lysophosphatidylcholine Micelles

Specificity in transmembrane helix–helix interactions can define a hierarchy of stability for sequence variants

On the thermodynamic stability of a charged arginine side chain in a transmembrane helix

Amide vibrations are delocalized across the hydrophobic interface of a transmembrane helix dimer