NMR paper The interactions of the HIV gp41 fusion peptides with zwitterionic membrane mimics de

		BioNMR > Educational resources > Journal club
[NMR paper] The interactions of the HIV gp41 fusion peptides with zwitterionic membrane mimics de

Webservers

NMR processing:

MDD

NMR assignment:

Backbone:

Side-chains:

NOEs:

Structure from NMR restraints:

Ab initio:

Fragment-based:

Rosetta-NMR (Robetta)

Template-based:

GeNMR

I-TASSER

Refinement:

Amber

Structure from chemical shifts:

Fragment-based:

Homology-based:

Torsion angles from chemical shifts:

Preditor

TALOS

Promega- Proline

Secondary structure from chemical shifts:

CSI (via RCI server)

TALOS

MICS caps, β-turns

d2D

PECAN

Flexibility from chemical shifts:

RCI

Interactions from chemical shifts:

HADDOCK

Chemical shifts re-referencing:

NMR model quality:

NOEs, other restraints:

Chemical shifts:

RDCs:

Pseudocontact shifts:

Protein geomtery:

SAVES2 or SAVES4

Quality Control Check

NMR spectrum prediction:

FANDAS

MestReS

V-NMR

Flexibility from structure:

Backbone S2

Methyl S2

B-factor

Molecular dynamics:

Gromacs

Amber

Antechamber

Chemical shifts prediction:

From structure:

Shiftx2

Sparta+

Camshift

CH3shift- Methyl

ArShift- Aromatic

ShiftS

Proshift

PPM

CheShift-2- Cα

From sequence:

Shifty

Camcoil

Poulsen_rc_CS

Disordered proteins:

MAXOCC

Format conversion & validation:

CCPN

From NMR-STAR 3.1

Validate NMR-STAR 3.1

NMR sample preparation:

Protein disorder:

DisMeta

Protein solubility:

Isotope labeling:

Solid-state NMR:

Thread Tools

Search this Thread

Rate Thread

Display Modes

11-24-2010, 10:03 PM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,732

Points: 193,617, Level: 100

Level up: 0%, 0 Points needed

Activity: 50.7%

Last Achievements

Award-Showcase

NMR Credits: 0

NMR Points: 193,617

Downloads: 0

Uploads: 0

The interactions of the HIV gp41 fusion peptides with zwitterionic membrane mimics de

The interactions of the HIV gp41 fusion peptides with zwitterionic membrane mimics determined by NMR spectroscopy.

Related Articles The interactions of the HIV gp41 fusion peptides with zwitterionic membrane mimics determined by NMR spectroscopy.

Biochim Biophys Acta. 2004 Nov 17;1667(1):67-81

Authors: Morris KF, Gao X, Wong TC

The wild-type (wt) N-terminal 23-residue fusion peptide (FP) of the human immunodeficiency virus (HIV) fusion protein gp41 and its V2E mutant have been studied by nuclear magnetic resonance (NMR) spectroscopy in dodecylphosphocholine (DPC) micelles as membrane mimics. A number of NMR techniques have been used. Pulsed field-gradient diffusion measurements in DPC and in 4:1 DPC/sodium dodecylsulfate mixed micelles showed that there is no major difference between the partition coefficients of the fusogenic wt peptide and the V2E mutant in these micelles, indicating that there is no correlation between the activity of the fusion peptides and their membrane affinities. The nuclear Overhauser enhancement (NOE) patterns and the chemical shift index for these two peptides indicated that both FP are in an alpha helical conformation between the Ile4 to Leu12 or to Ala15 region. Simulated annealing showed that the helical region extends from Ile4 to Met19. The two FPs share similar conformational characteristics, indicating that the conformation of the FP is not an important factor determining its activity. The spin-label studies, utilizing spin labels 5- and 16-doxystearic acids in the DPC micelles, provided clear indication that the wt FP inserts its N-terminus into the micelles while the V2E mutant does not insert into the micelles. The conclusion from the spin-label results is corroborated by deuterium amide proton exchange experiments. The correlation between the oblique insertion of the FP and its fusogenic activity is in excellent agreement with results from our molecular dynamics simulation and from other previous studies.

PMID: 15533307 [PubMed - indexed for MEDLINE]

Source: PubMed

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
Conformational Disorder of Membrane Peptides Investigated from Solid-State NMR Linewidths and Lineshapes. Conformational Disorder of Membrane Peptides Investigated from Solid-State NMR Linewidths and Lineshapes. Conformational Disorder of Membrane Peptides Investigated from Solid-State NMR Linewidths and Lineshapes. J Phys Chem B. 2011 Aug 1; Authors: Su Y, Hong M A challenge in the application of solid-state NMR spectroscopy to membrane proteins and peptides is the relatively broad linewidths compared to solution NMR spectra. To understand the linewidth contributions to membrane protein spectra, we have measured the inhomogeneous and homogeneous...	nmrlearner	Journal club	0	08-03-2011 12:00 PM
Solid-state NMR of amyloid membrane interactions. Solid-state NMR of amyloid membrane interactions. Solid-state NMR of amyloid membrane interactions. Methods Mol Biol. 2011;752:165-77 Authors: Gehman JD, Separovic F Solid-state NMR pulse sequences often feature fewer pulses and delays than the more common solution NMR experiments. This ostensible simplicity, however, belies the care with which experimental parameters must be determined, as solid-state NMR can be much less forgiving of improper experimental set-up. This is especially true of "semi-solid" samples, such as the phospholipid vesicles...	nmrlearner	Journal club	0	06-30-2011 01:24 PM
Structure and dynamics of cationic membrane peptides and proteins: Insights from solid-state NMR. Structure and dynamics of cationic membrane peptides and proteins: Insights from solid-state NMR. Structure and dynamics of cationic membrane peptides and proteins: Insights from solid-state NMR. Protein Sci. 2011 Feb 22; Authors: Hong M, Su Y Many membrane peptides and protein domains contain functionally important cationic Arg and Lys residues, whose insertion into the hydrophobic interior of the lipid bilayer encounters significant energy barriers. To understand how these cationic molecules overcome the free energy barrier to insert into the...	nmrlearner	Journal club	0	02-24-2011 11:04 AM
[NMR paper] Conformational study of fragments of envelope proteins (gp120: 254-274 and gp41: 519- Conformational study of fragments of envelope proteins (gp120: 254-274 and gp41: 519-541) of HIV-1 by NMR and MD simulations. Related Articles Conformational study of fragments of envelope proteins (gp120: 254-274 and gp41: 519-541) of HIV-1 by NMR and MD simulations. J Pept Sci. 2004 Jun;10(6):363-80 Authors: Kanyalkar M, Srivastava S, Saran A, Coutinho E The envelope proteins, gp 120 and gp41 of HIV-1, play a crucial role in receptor (CD4+ lymphocytes) binding and membrane fusion. The fragment 254-274 of gp120 is conserved in all strains of...	nmrlearner	Journal club	0	11-24-2010 09:51 PM
[NMR paper] Probing membrane surfaces and the location of membrane-embedded peptides by (13)C MAS Probing membrane surfaces and the location of membrane-embedded peptides by (13)C MAS NMR using lanthanide ions. Related Articles Probing membrane surfaces and the location of membrane-embedded peptides by (13)C MAS NMR using lanthanide ions. J Magn Reson. 1999 Dec;141(2):335-9 Authors: Gröbner G, Glaubitz C, Watts A A simple but efficient (13)C MAS NMR method is presented for the determination of the location of embedded molecules such as peptides relative to biological membrane surfaces by exploiting the interaction with paramagnetic...	nmrlearner	Journal club	0	11-18-2010 08:31 PM
[NMR paper] NMR studies of a viral protein that mimics the regulators of complement activation. NMR studies of a viral protein that mimics the regulators of complement activation. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR studies of a viral protein that mimics the regulators of complement activation. J Mol Biol. 1997 Sep 19;272(2):253-65 Authors: Wiles AP, Shaw G, Bright J, Perczel A, Campbell ID, Barlow PN Vaccinia virus complement control protein (VCP) is a 243-residue protein that is similar in sequence to the regulators of complement activation; its...	nmrlearner	Journal club	0	08-22-2010 05:08 PM
[NMR paper] A high-resolution 1H NMR approach for structure determination of membrane peptides an A high-resolution 1H NMR approach for structure determination of membrane peptides and proteins in non-deuterated detergent: application to mastoparan X solubilized in n-octylglucoside. Related Articles A high-resolution 1H NMR approach for structure determination of membrane peptides and proteins in non-deuterated detergent: application to mastoparan X solubilized in n-octylglucoside. J Biomol NMR. 1995 Jun;5(4):345-52 Authors: Seigneuret M, LÃ©vy D Application of 1H 2D NMR methods to solubilized membrane proteins and peptides has up to now...	nmrlearner	Journal club	0	08-22-2010 03:41 AM
Solid State NMR of membrane peptides and proteins Solid State NMR of membrane peptides and proteins Lecture notes on "Solid State NMR of membrane peptides and proteins" by Dr. SK Straus from Univ. of British Columbia More...	nmrlearner	General	0	08-16-2010 03:50 AM

« Previous Thread | Next Thread »

Posting Rules
You may not post new threads You may not post replies You may not post attachments You may not edit your posts BB code is On Smilies are On [IMG] code is On HTML code is On Trackbacks are Off Pingbacks are Off Refbacks are Off