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 08-22-2010, 03:03 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,732
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 1H, 15N and 13C NMR assignments, secondary structure and overall topology of the Esch

1H, 15N and 13C NMR assignments, secondary structure and overall topology of the Escherichia coli GlgS protein.

Related Articles 1H, 15N and 13C NMR assignments, secondary structure and overall topology of the Escherichia coli GlgS protein.

Eur J Biochem. 1997 Jun 1;246(2):301-10

Authors: Beglova N, Fischer D, Hengge-Aronis R, Gehring K

GlgS is a 7892-Da protein which is involved in glycogen biosynthesis in bacteria. We report the 1H, 15N and 13C NMR assignments of the backbone and side-chain resonances at 25 degrees C and pH 6.7 from two-dimensional homonuclear and three-dimensional heteronuclear NMR experiments. The secondary structure of the protein was determined using sequential and medium-range NOE correlations, vicinal 3J(NH-H alpha) coupling values and amide proton exchange rates. The secondary structure obtained is consistent with the secondary chemical shifts of 1H alpha, 13C alpha and 13C = O. It was found that the secondary structure of GlgS comprises two amphipathic helices (Asn10-Met21 and Glu39-Arg60), one short highly hydrophobic helix (Ile30-Val33), a short extended beta-strand-like fragment (Arg26-Asp29) and two type I beta-turns (His22-Gly25 and Thr34-Met37). An overall topology of GlgS is suggested based on long-range NOEs. The elements of secondary structure form a sandwich in which the beta-strand and the short hydrophobic helix are positioned between the two amphipathic helices.

PMID: 9208918 [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] 1H, 15N and 13C NMR assignments, secondary structure and overall topology of the Esch
1H, 15N and 13C NMR assignments, secondary structure and overall topology of the Escherichia coli GlgS protein. 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 1H, 15N and 13C NMR assignments, secondary structure and overall topology of the Escherichia coli GlgS protein. Eur J Biochem. 1997 Jun 1;246(2):301-10 Authors: Beglova N, Fischer D, Hengge-Aronis R, Gehring K GlgS is a 7892-Da protein which is involved in glycogen...
nmrlearner Journal club 0 08-22-2010 03:31 PM
[NMR paper] Primary structure, sequence-specific 1H-NMR assignments and secondary structure in so
Primary structure, sequence-specific 1H-NMR assignments and secondary structure in solution of bromelain inhibitor VI from pineapple stem. 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 Primary structure, sequence-specific 1H-NMR assignments and secondary structure in solution of bromelain inhibitor VI from pineapple stem. Eur J Biochem. 1995 Sep 1;232(2):335-43 Authors: Hatano K, Kojima M, Tanokura M, Takahashi K One of the...
nmrlearner Journal club 0 08-22-2010 03:50 AM
[NMR paper] Complete 1H, 13C and 15N NMR assignments and secondary structure of the 269-residue s
Complete 1H, 13C and 15N NMR assignments and secondary structure of the 269-residue serine protease PB92 from Bacillus alcalophilus. Related Articles Complete 1H, 13C and 15N NMR assignments and secondary structure of the 269-residue serine protease PB92 from Bacillus alcalophilus. J Biomol NMR. 1995 Apr;5(3):259-70 Authors: Fogh RH, Schipper D, Boelens R, Kaptein R The 1H, 13C and 15N NMR resonances of serine protease PB92 have been assigned using 3D triple-resonance NMR techniques. With a molecular weight of 27 kDa (269 residues) this...
nmrlearner Journal club 0 08-22-2010 03:41 AM
[NMR paper] 1H, 13C and 15N NMR backbone assignments and secondary structure of the 269-residue p
1H, 13C and 15N NMR backbone assignments and secondary structure of the 269-residue protease subtilisin 309 from Bacillus lentus. Related Articles 1H, 13C and 15N NMR backbone assignments and secondary structure of the 269-residue protease subtilisin 309 from Bacillus lentus. J Biomol NMR. 1994 Mar;4(2):257-78 Authors: Remerowski ML, Domke T, Groenewegen A, Pepermans HA, Hilbers CW, van de Ven FJ 1H, 13C and 15N NMR assignments of the backbone atoms of subtilisin 309, secreted by Bacillus lentus, have been made using heteronuclear 3D NMR...
nmrlearner Journal club 0 08-22-2010 03:33 AM
[NMR paper] 1H, 13C and 15N NMR backbone assignments and secondary structure of the 269-residue p
1H, 13C and 15N NMR backbone assignments and secondary structure of the 269-residue protease subtilisin 309 from Bacillus lentus. Related Articles 1H, 13C and 15N NMR backbone assignments and secondary structure of the 269-residue protease subtilisin 309 from Bacillus lentus. J Biomol NMR. 1994 Mar;4(2):257-78 Authors: Remerowski ML, Domke T, Groenewegen A, Pepermans HA, Hilbers CW, van de Ven FJ 1H, 13C and 15N NMR assignments of the backbone atoms of subtilisin 309, secreted by Bacillus lentus, have been made using heteronuclear 3D NMR...
nmrlearner Journal club 0 08-22-2010 03:33 AM
[NMR paper] 1H resonance assignments, secondary structure and general topology of single-chain mo
1H resonance assignments, secondary structure and general topology of single-chain monellin in solution as determined by 1H 2D-NMR. Related Articles 1H resonance assignments, secondary structure and general topology of single-chain monellin in solution as determined by 1H 2D-NMR. J Biomol NMR. 1992 Nov;2(6):557-72 Authors: Tomic MT, Somoza JR, Wemmer DE, Park YW, Cho JM, Kim SH We determined the resonance assignments, secondary structure and general topology of the 11-kDa sweet protein single-chain monellin (SCM), using two-dimensional proton...
nmrlearner Journal club 0 08-21-2010 11:45 PM
[NMR paper] Secondary structure and topology of interleukin-1 receptor antagonist protein determi
Secondary structure and topology of interleukin-1 receptor antagonist protein determined by heteronuclear three-dimensional NMR spectroscopy. Related Articles Secondary structure and topology of interleukin-1 receptor antagonist protein determined by heteronuclear three-dimensional NMR spectroscopy. Biochemistry. 1992 Jun 16;31(23):5237-45 Authors: Stockman BJ, Scahill TA, Roy M, Ulrich EL, Strakalaitis NA, Brunner DP, Yem AW, Deibel MR Interleukin-1 (IL-1) proteins, such as IL-1 beta, play a key role in immune and inflammatory responses....
nmrlearner Journal club 0 08-21-2010 11:41 PM
[NMR paper] Determination of the secondary structure and molecular topology of interleukin-1 beta
Determination of the secondary structure and molecular topology of interleukin-1 beta by use of two- and three-dimensional heteronuclear 15N-1H NMR spectroscopy. Related Articles Determination of the secondary structure and molecular topology of interleukin-1 beta by use of two- and three-dimensional heteronuclear 15N-1H NMR spectroscopy. Biochemistry. 1990 May 15;29(19):4668-82 Authors: Driscoll PC, Gronenborn AM, Wingfield PT, Clore GM A study of the regular secondary structure elements of recombinant human interleukin-1 beta has been...
nmrlearner Journal club 0 08-21-2010 10:48 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 09:37 PM.


Map