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, 11:04 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 17,583
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 Assignment of the backbone 1H and 15N NMR resonances of bacteriophage T4 lysozyme.

Assignment of the backbone 1H and 15N NMR resonances of bacteriophage T4 lysozyme.

Related Articles Assignment of the backbone 1H and 15N NMR resonances of bacteriophage T4 lysozyme.

Biochemistry. 1990 Jul 10;29(27):6341-62

Authors: McIntosh LP, Wand AJ, Lowry DF, Redfield AG, Dahlquist FW

The proton and nitrogen (15NH-H alpha-H beta) resonances of bacteriophage T4 lysozyme were assigned by 15N-aided 1H NMR. The assignments were directed from the backbone amide 1H-15N nuclei, with the heteronuclear single-multiple-quantum coherence (HSMQC) spectrum of uniformly 15N enriched protein serving as the master template for this work. The main-chain amide 1H-15N resonances and H alpha resonances were resolved and classified into 18 amino acid types by using HMQC and 15N-edited COSY measurements, respectively, of T4 lysozymes selectively enriched with one or more of alpha-15N-labeled Ala, Arg, Asn, Asp, Gly, Gln, Glu, Ile, Leu, Lys, Met, Phe, Ser, Thr, Trp, Tyr, or Val. The heteronuclear spectra were complemented by proton DQF-COSY and TOCSY spectra of unlabeled protein in H2O and D2O buffers, from which the H beta resonances of many residues were identified. The NOE cross peaks to almost every amide proton were resolved in 15N-edited NOESY spectra of the selectively 15N enriched protein samples. Residue specific assignments were determined by using NOE connectivities between protons in the 15NH-H alpha-H beta spin systems of known amino acid type. Additional assignments of the aromatic proton resonances were obtained from 1H NMR spectra of unlabeled and selectively deuterated protein samples. The secondary structure of T4 lysozyme indicated from a qualitative analysis of the NOESY data is consistent with the crystallographic model of the protein.

PMID: 2207079 [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] Dynamics of xenon binding inside the hydrophobic cavity of pseudo-wild-type bacteriophage T4 lysozyme explored through xenon-based NMR spectroscopy.
Dynamics of xenon binding inside the hydrophobic cavity of pseudo-wild-type bacteriophage T4 lysozyme explored through xenon-based NMR spectroscopy. Related Articles Dynamics of xenon binding inside the hydrophobic cavity of pseudo-wild-type bacteriophage T4 lysozyme explored through xenon-based NMR spectroscopy. J Am Chem Soc. 2005 Aug 24;127(33):11676-83 Authors: Desvaux H, Dubois L, Huber G, Quillin ML, Berthault P, Matthews BW Wild-type bacteriophage T4 lysozyme contains a hydrophobic cavity with binding properties that have been...
nmrlearner Journal club 0 12-01-2010 06:56 PM
[NMR paper] NMR assignment of the gpU tail protein from lambda bacteriophage.
NMR assignment of the gpU tail protein from lambda bacteriophage. Related Articles NMR assignment of the gpU tail protein from lambda bacteriophage. J Biomol NMR. 2005 May;32(1):91-2 Authors: Edmonds L, Thirumoorthy R, Liu A, Davidson A, Donaldson L
nmrlearner Journal club 0 11-25-2010 08:21 PM
[NMR paper] NMR structure of Citrobacter freundii AmpD, comparison with bacteriophage T7 lysozyme
NMR structure of Citrobacter freundii AmpD, comparison with bacteriophage T7 lysozyme and homology with PGRP domains. Related Articles NMR structure of Citrobacter freundii AmpD, comparison with bacteriophage T7 lysozyme and homology with PGRP domains. J Mol Biol. 2003 Apr 4;327(4):833-42 Authors: Liepinsh E, Généreux C, Dehareng D, Joris B, Otting G AmpD is a bacterial amidase involved in the recycling of cell-wall fragments in Gram-negative bacteria. Inactivation of AmpD leads to derepression of beta-lactamase expression, presenting a major...
nmrlearner Journal club 0 11-24-2010 09:01 PM
[NMR paper] What is the average conformation of bacteriophage T4 lysozyme in solution? A domain o
What is the average conformation of bacteriophage T4 lysozyme in solution? A domain orientation study using dipolar couplings measured by solution NMR. Related Articles What is the average conformation of bacteriophage T4 lysozyme in solution? A domain orientation study using dipolar couplings measured by solution NMR. J Mol Biol. 2001 May 11;308(4):745-64 Authors: Goto NK, Skrynnikov NR, Dahlquist FW, Kay LE Lysozyme from T4 bacteriophage is comprised of two domains that are both involved in binding substrate. Although wild-type lysozyme has...
nmrlearner Journal club 0 11-19-2010 08:32 PM
[NMR paper] Assignment of the backbone 1H,15N,13C NMR resonances and secondary structure of a dou
Assignment of the backbone 1H,15N,13C NMR resonances and secondary structure of a double-stranded RNA binding domain from the Drosophila protein staufen. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Assignment of the backbone 1H,15N,13C NMR resonances and secondary structure of a double-stranded RNA binding domain from the Drosophila protein staufen. FEBS Lett. 1995 Apr 10;362(3):333-6 Authors: Bycroft M, Proctor M, Freund SM, St Johnston D NMR spectroscopy has been...
nmrlearner Journal club 0 08-22-2010 03:41 AM
[NMR paper] Sequence-specific assignments of the backbone 1H, 13C, and 15N resonances of the MutT
Sequence-specific assignments of the backbone 1H, 13C, and 15N resonances of the MutT enzyme by heteronuclear multidimensional NMR. Related Articles Sequence-specific assignments of the backbone 1H, 13C, and 15N resonances of the MutT enzyme by heteronuclear multidimensional NMR. Biochemistry. 1993 Dec 7;32(48):13071-80 Authors: Abeygunawardana C, Weber DJ, Frick DN, Bessman MJ, Mildvan AS The MutT protein, a 129-residue enzyme from Escherichia coli which prevents A.T-->C.G mutations, catalyzes the hydrolysis of nucleoside triphosphates (NTP)...
nmrlearner Journal club 0 08-22-2010 03:01 AM
[NMR paper] Assignment of the backbone 1H and 15N NMR resonances and secondary structure characte
Assignment of the backbone 1H and 15N NMR resonances and secondary structure characterization of barstar. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Assignment of the backbone 1H and 15N NMR resonances and secondary structure characterization of barstar. FEBS Lett. 1993 Oct 11;332(1-2):81-7 Authors: Lubienski MJ, Bycroft M, Jones DN, Fersht AR Barstar, a polypeptide inhibitor of ribonucleases, has been studied by 2D and 3D NMR techniques using uniformly...
nmrlearner Journal club 0 08-22-2010 03:01 AM
[NMR paper] Assignment of 1H, 15N, and backbone 13C resonances in detergent-solubilized M13 coat
Assignment of 1H, 15N, and backbone 13C resonances in detergent-solubilized M13 coat protein via multinuclear multidimensional NMR: a model for the coat protein monomer. Related Articles Assignment of 1H, 15N, and backbone 13C resonances in detergent-solubilized M13 coat protein via multinuclear multidimensional NMR: a model for the coat protein monomer. Biochemistry. 1993 Aug 17;32(32):8322-8 Authors: van de Ven FJ, van Os JW, Aelen JM, Wymenga SS, Remerowski ML, Konings RN, Hilbers CW The major coat protein (gVIIIp) of bacteriophage M13...
nmrlearner Journal club 0 08-22-2010 03:01 AM


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 - 2017, 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 05:39 PM.


Map