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



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  
Unread 08-21-2010, 11:41 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,135
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 The secondary structure of the colicin E3 immunity protein as studied by 1H-1H and 1H

The secondary structure of the colicin E3 immunity protein as studied by 1H-1H and 1H-15N two-dimensional NMR spectroscopy.

Related Articles The secondary structure of the colicin E3 immunity protein as studied by 1H-1H and 1H-15N two-dimensional NMR spectroscopy.

Biochemistry. 1992 Jun 23;31(24):5578-86

Authors: Yajima S, Muto Y, Yokoyama S, Masaki H, Uozumi T

By performing 1H-1H and 1H-15N two-dimensional (2D) nuclear magnetic resonance (NMR) experiments, the complete sequence-specific resonance assignment was determined for the colicin E3 immunity protein (84 residues; ImmE3), which binds to colicin E3 and inhibits its RNase activity. First, the fingerprint region of the spectrum was analyzed by homonuclear 1H-1H HOHAHA and NOESY methods. For the identification of overlapping resonances, heteronuclear 1H-15N (HMQC-HOHAHA, HMQC-NOESY) experiments were performed, so that the complete 1H and 15N resonance assignments were provided. Then the secondary structure of ImmE3 was determined by examination of characteristic patterns of sequential backbone proton NOEs in combination with measurement of exchange rates of amide protons and 3JHN alpha coupling constants. From these results, it was concluded that ImmE3 contains a four-stranded antiparallel beta-sheet (residues 2-10, 19-22, 47-49, and 71-79) and a short alpha-helix (residues 31-36).

PMID: 1610804 [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] Large structure rearrangement of colicin ia channel domain after membrane binding fro
Large structure rearrangement of colicin ia channel domain after membrane binding from 2D 13C spin diffusion NMR. Related Articles Large structure rearrangement of colicin ia channel domain after membrane binding from 2D 13C spin diffusion NMR. J Am Chem Soc. 2005 May 4;127(17):6402-8 Authors: Luo W, Yao X, Hong M One of the main mechanisms of membrane protein folding is by spontaneous insertion into the lipid bilayer from the aqueous environment. The bacterial toxin, colicin Ia, is one such protein. To shed light on the conformational changes...
nmrlearner Journal club 0 11-25-2010 08:21 PM
[NMR paper] NMR solution structure of ImB2, a protein conferring immunity to antimicrobial activi
NMR solution structure of ImB2, a protein conferring immunity to antimicrobial activity of the type IIa bacteriocin, carnobacteriocin B2. Related Articles NMR solution structure of ImB2, a protein conferring immunity to antimicrobial activity of the type IIa bacteriocin, carnobacteriocin B2. Biochemistry. 2004 Sep 21;43(37):11740-9 Authors: Sprules T, Kawulka KE, Vederas JC Bacteriocins produced by lactic acid bacteria are potent antimicrobial compounds which are active against closely related bacteria. Producer strains are protected against...
nmrlearner Journal club 0 11-24-2010 10:01 PM
[NMR paper] Structure of the model peptides of Bombyx mori silk-elastin like protein studied with
Structure of the model peptides of Bombyx mori silk-elastin like protein studied with solid state NMR. Related Articles Structure of the model peptides of Bombyx mori silk-elastin like protein studied with solid state NMR. Biomacromolecules. 2004 May-Jun;5(3):744-50 Authors: Ohgo K, Kurano TL, Kumashiro KK, Asakura T The peptides (AG)(6)(VPGVG)(AG)(7) and (AG)(5)(VPGVG)(2)(AG)(5) are models for a new type of protein with both composition and properties such as Bombyx mori silk and elastin. In this paper, we report the solid-state NMR results...
nmrlearner Journal club 0 11-24-2010 09:51 PM
[NMR paper] NMR trial models: experiences with the colicin immunity protein Im7 and the p85alpha
NMR trial models: experiences with the colicin immunity protein Im7 and the p85alpha C-terminal SH2-peptide complex. Related Articles NMR trial models: experiences with the colicin immunity protein Im7 and the p85alpha C-terminal SH2-peptide complex. Acta Crystallogr D Biol Crystallogr. 2001 Oct;57(Pt 10):1397-404 Authors: Pauptit RA, Dennis CA, Derbyshire DJ, Breeze AL, Weston SA, Rowsell S, Murshudov GN Two cases of successful molecular replacement using NMR trial models are presented. One is the crystal structure of the Escherichia coli...
nmrlearner Journal club 0 11-19-2010 08:44 PM
[NMR paper] NMR secondary structure of the plasminogen activator protein staphylokinase.
NMR secondary structure of the plasminogen activator protein staphylokinase. Related Articles NMR secondary structure of the plasminogen activator protein staphylokinase. J Biomol NMR. 1997 Apr;9(3):273-86 Authors: Ohlenschläger O, Ramachandran R, Flemming J, Gührs KH, Schlott B, Brown LR Staphylokinase (Sak) is a 15.5 kDa protein secreted by several strains of Staphylococcus aureus. Due to its ability to convert plasminogen, the inactive proenzyme of the fibrinolytic system, into plasmin, Sak is presently undergoing clinical trials for...
nmrlearner Journal club 0 08-22-2010 03:31 PM
[NMR paper] NMR secondary structure of the plasminogen activator protein staphylokinase.
NMR secondary structure of the plasminogen activator protein staphylokinase. Related Articles NMR secondary structure of the plasminogen activator protein staphylokinase. J Biomol NMR. 1997 Apr;9(3):273-86 Authors: Ohlenschläger O, Ramachandran R, Flemming J, Gührs KH, Schlott B, Brown LR Staphylokinase (Sak) is a 15.5 kDa protein secreted by several strains of Staphylococcus aureus. Due to its ability to convert plasminogen, the inactive proenzyme of the fibrinolytic system, into plasmin, Sak is presently undergoing clinical trials for...
nmrlearner Journal club 0 08-22-2010 03:03 PM
[NMR paper] Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using
Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptide. Related Articles Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptide. Biochemistry. 1992 Sep 22;31(37):8790-8 Authors: Sönnichsen FD, Van Eyk JE, Hodges RS, Sykes BD The structure of a synthetic peptide comprising the 28 amino-terminal residues of actin has been examined by 1H-NMR and CD spectroscopy. The peptide is largely unstructured and flexible in solution but becomes...
nmrlearner Journal club 0 08-21-2010 11:45 PM
PECAN server - protein secondary structure via NMR
http://bija.nmrfam.wisc.edu/PECAN/Pecan.jpg Link to the PECAN server Instructions about PECAN input files Info from the PECAN website:PECAN offers a new approach to secondary structure identification that achieves excellent results. PECAN is a component in a suite of tools for high-throughput structure determination using NMR.
nmrlearner NMR software 0 07-20-2005 05:44 PM


Thread Tools Search this Thread
Search this Thread:

Advanced Search
Display Modes Rate This Thread
Rate This 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



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 05:04 AM.


Map