BioNMR
NMR aggregator & online community since 2003
BioNMR    
Learn or help to learn NMR - get free NMR books!
 

Go Back   BioNMR > Educational resources > Journal club
Advanced Search
Home Forums Wiki NMR feeds Downloads Register Today's Posts



Jobs Groups Conferences Literature Pulse sequences Software forums Programs Sample preps Web resources BioNMR issues


Webservers
NMR processing:
MDD
NMR assignment:
Backbone:
Autoassign
MARS
UNIO Match
PINE
Side-chains:
UNIO ATNOS-Ascan
NOEs:
UNIO ATNOS-Candid
UNIO Candid
ASDP
Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
XPLOR-NIH
ASDP
UNIO ATNOS-Candid
UNIO Candid
Fragment-based:
BMRB CS-Rosetta
Rosetta-NMR (Robetta)
Template-based:
GeNMR
I-TASSER
Refinement:
Amber
Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
BMRB CS-Rosetta
Homology-based:
CS23D
Simshift
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:
Shiftcor
UNIO Shiftinspector
LACS
CheckShift
RefDB
NMR model quality:
NOEs, other restraints:
PROSESS
PSVS
RPF scores
iCing
Chemical shifts:
PROSESS
CheShift2
Vasco
iCing
RDCs:
DC
Anisofit
Pseudocontact shifts:
Anisofit
Protein geomtery:
Resolution-by-Proxy
PROSESS
What-If
iCing
PSVS
MolProbity
SAVES2 or SAVES4
Vadar
Prosa
ProQ
MetaMQAPII
PSQS
Eval123D
STAN
Ramachandran Plot
Rampage
ERRAT
Verify_3D
Harmony
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:
camLILA
ccSOL
Camfold
camGroEL
Zyggregator
Isotope labeling:
UPLABEL
Solid-state NMR:
sedNMR


Reply
 
Thread Tools Search this Thread Rate Thread Display Modes
  #1  
Old 11-19-2010, 08:32 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,734
Points: 193,617, Level: 100
Points: 193,617, Level: 100 Points: 193,617, Level: 100 Points: 193,617, Level: 100
Level up: 0%, 0 Points needed
Level up: 0% Level up: 0% Level up: 0%
Activity: 50.7%
Activity: 50.7% Activity: 50.7% Activity: 50.7%
Last Achievements
Award-Showcase
NMR Credits: 0
NMR Points: 193,617
Downloads: 0
Uploads: 0
Default Solid state NMR measurements of conformation and conformational distributions in the

Solid state NMR measurements of conformation and conformational distributions in the membrane-bound HIV-1 fusion peptide.

Related Articles Solid state NMR measurements of conformation and conformational distributions in the membrane-bound HIV-1 fusion peptide.

J Mol Graph Model. 2001;19(1):129-35

Authors: Yang J, Parkanzky PD, Khunte BA, Canlas CG, Yang R, Gabrys CM, Weliky DP

The solid state NMR lineshape of a protein backbone carbonyl nucleus is a general diagnostic of the local conformational distribution in the vicinity of that nucleus. In addition, measurements of carbonyl chemical shifts and 2D exchange spectra provide information about the most probable conformation in the distribution. These types of solid state NMR methodologies have been applied to structural studies of the membrane-bound HIV-1 fusion peptide. This peptide is derived from a domain of the HIV-1 gp41 envelope protein, which is critical for viral-host cell-membrane fusion. Even in the absence of the rest of the envelope protein, the fusion peptide will fuse liposomes or erythrocytes. The solid state NMR measurements demonstrate that the center of the membrane-bound HIV-1 fusion peptide is structured, while the C-terminus is highly disordered. The structural distribution at the peptide center is lipid-dependent, with the greatest degree of structural homogeneity in a lipid environment whose composition reflects that of the target T cells. When bound to the lipid mixture, the peptide center is predominately beta sheet. The beta-sheet structure may be diagnostic of peptide oligomerization, which is thought to be a requirement for membrane fusion activity. Although the peptide partially disrupts bilayer orientational ordering in stacked glass-plate samples, 2H NMR demonstrates that the bilayers remain intact in the presence of the fusion peptide and are not micellized. The retention of the bilayer phase may relate to the biological requirement that the virus should fuse with, but not destroy, the target host cell membrane.

PMID: 11381522 [PubMed - indexed for MEDLINE]



Source: PubMed
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
[NMR paper] Solid-state NMR measurements of the kinetics of the interaction between phospholamban and Ca2+-ATPase in lipid bilayers.
Solid-state NMR measurements of the kinetics of the interaction between phospholamban and Ca2+-ATPase in lipid bilayers. Related Articles Solid-state NMR measurements of the kinetics of the interaction between phospholamban and Ca2+-ATPase in lipid bilayers. Mol Membr Biol. 2005 Jul-Aug;22(4):353-61 Authors: Hughes E, Middleton DA Phospholamban (PLB) is a small transmembrane protein that regulates calcium transport across the sarcoplasmic reticulum (SR) of cardiac cells via a reversible inhibitory interaction with Ca2+-ATPase. In this work...
nmrlearner Journal club 0 12-01-2010 06:56 PM
[NMR paper] Probing site-specific conformational distributions in protein folding with solid-stat
Probing site-specific conformational distributions in protein folding with solid-state NMR. Related Articles Probing site-specific conformational distributions in protein folding with solid-state NMR. Proc Natl Acad Sci U S A. 2005 Mar 1;102(9):3284-9 Authors: Havlin RH, Tycko R We demonstrate an experimental approach to structural studies of unfolded and partially folded proteins in which conformational distributions are probed at a site-specific level by 2D solid-state 13C NMR spectroscopy of glassy frozen solutions. Experiments on chemical...
nmrlearner Journal club 0 11-24-2010 11:14 PM
[NMR paper] Synthesis, enhanced fusogenicity, and solid state NMR measurements of cross-linked HI
Synthesis, enhanced fusogenicity, and solid state NMR measurements of cross-linked HIV-1 fusion peptides. Related Articles Synthesis, enhanced fusogenicity, and solid state NMR measurements of cross-linked HIV-1 fusion peptides. Biochemistry. 2003 Apr 1;42(12):3527-35 Authors: Yang R, Yang J, Weliky DP In the HIV-1 gp41 and other viral fusion proteins, the minimal oligomerization state is believed to be trimeric with three N-terminal fusion peptides inserting into the membrane in close proximity. Previous studies have demonstrated that the...
nmrlearner Journal club 0 11-24-2010 09:01 PM
[NMR paper] Practical methods for solid-state NMR distance measurements on large biomolecules: co
Practical methods for solid-state NMR distance measurements on large biomolecules: constant-time rotational resonance. Related Articles Practical methods for solid-state NMR distance measurements on large biomolecules: constant-time rotational resonance. J Magn Reson. 1999 Aug;139(2):371-6 Authors: Balazs YS, Thompson LK Simple modifications of the rotational resonance experiment substantially reduce the total experimental time needed to measure weak homonuclear dipolar couplings, a critical factor for achieving routine internuclear distance...
nmrlearner Journal club 0 11-18-2010 08:31 PM
[NMR paper] Solid-state REDOR NMR distance measurements at the ligand site of a bacterial chemota
Solid-state REDOR NMR distance measurements at the ligand site of a bacterial chemotaxis membrane receptor. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Solid-state REDOR NMR distance measurements at the ligand site of a bacterial chemotaxis membrane receptor. Biochemistry. 1997 Feb 18;36(7):1699-703 Authors: Wang J, Balazs YS, Thompson LK The Escherichia coli serine receptor senses serine levels in the environment and transmits this information across the bacterial inner membrane to...
nmrlearner Journal club 0 08-22-2010 03:31 PM
[NMR paper] Solid-state REDOR NMR distance measurements at the ligand site of a bacterial chemota
Solid-state REDOR NMR distance measurements at the ligand site of a bacterial chemotaxis membrane receptor. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Solid-state REDOR NMR distance measurements at the ligand site of a bacterial chemotaxis membrane receptor. Biochemistry. 1997 Feb 18;36(7):1699-703 Authors: Wang J, Balazs YS, Thompson LK The Escherichia coli serine receptor senses serine levels in the environment and transmits this information across the bacterial inner membrane to...
nmrlearner Journal club 0 08-22-2010 03:03 PM
[NMR paper] 31P solid-state NMR measurements used to detect interactions between NADPH and water
31P solid-state NMR measurements used to detect interactions between NADPH and water and to determine the ionisation state of NADPH in a protein-ligand complex subjected to low-level hydration. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles 31P solid-state NMR measurements used to detect interactions between NADPH and water and to determine the ionisation state of NADPH in a protein-ligand complex subjected to low-level hydration. Eur J Biochem. 1996 Jan...
nmrlearner Journal club 0 08-22-2010 02:27 PM
[NMR paper] Analysis of side-chain conformational distributions in neutrophil peptide-5 NMR struc
Analysis of side-chain conformational distributions in neutrophil peptide-5 NMR structures. Related Articles Analysis of side-chain conformational distributions in neutrophil peptide-5 NMR structures. Biopolymers. 1990 Dec;29(14):1807-22 Authors: Kominos D, Bassolino DA, Levy RM, Pardi A The side-chain conformations have been analyzed in the antimicrobial peptide, Neutrophil Peptide-5 (NP-5), whose structure was independently generated from nmr-derived distance constraints using a distance geometry algorithm. The side-chain and peptide...
nmrlearner Journal club 0 08-21-2010 11:04 PM



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



BioNMR advertisements to pay for website hosting and domain registration. Nobody does it for us.



Powered by vBulletin® Version 3.7.3
Copyright ©2000 - 2024, Jelsoft Enterprises Ltd.
Copyright, BioNMR.com, 2003-2013
Search Engine Friendly URLs by vBSEO 3.6.0

All times are GMT. The time now is 09:17 PM.


Map