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 01-09-2011, 12:46 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 17,256
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 Recent advances in segmental isotope labeling of proteins: NMR applications to large proteins and glycoproteins

Recent advances in segmental isotope labeling of proteins: NMR applications to large proteins and glycoproteins


Abstract In the last 15 years substantial advances have been made to place isotope labels in native and glycosylated proteins for NMR studies and structure determination. Key developments include segmental isotope labeling using Native Chemical Ligation, Expressed Protein Ligation and Protein Trans-Splicing. These advances are pushing the size limit of NMR spectroscopy further making larger proteins accessible for this technique. It is just emerging that segmental isotope labeling can be used to define inter-domain interactions in NMR structure determination. Labeling of post-translational modified proteins like glycoproteins remains difficult but some promising developments were recently achieved. Key achievements are segmental and site-specific labeling schemes that improve resonance assignment and structure determination of the glycan moiety. We adjusted the focus of this perspective article to concentrate on the NMR applications based on recent developments rather than on labeling methods themselves to illustrate the considerable potential for biomolecular NMR.
  • Content Type Journal Article
  • Pages 51-65
  • DOI 10.1007/s10858-009-9362-7
  • Authors
    • Lenka Skrisovska, ETH Zürich Institute for Molecular Biology and Biophysics 8093 Zurich Switzerland
    • Mario Schubert, ETH Zürich Institute for Molecular Biology and Biophysics 8093 Zurich Switzerland
    • Frédéric H.-T. Allain, ETH Zürich Institute for Molecular Biology and Biophysics 8093 Zurich Switzerland

Source: Journal of Biomolecular NMR
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
A segmental labeling strategy for unambiguous determination of domain??domain interactions of large multi-domain proteins
A segmental labeling strategy for unambiguous determination of domain??domain interactions of large multi-domain proteins Abstract NMR structural determination of large multi-domain proteins is a challenging task due to significant spectral overlap with a particular difficulty in unambiguous identification of domain??domain interactions. Segmental labeling is a NMR strategy that allows for isotopically labeling one domain and leaves the other domain unlabeled. This significantly simplifies spectral overlaps and allows for quick identification of domain??domain interaction. Here, a...
nmrlearner Journal club 0 07-08-2011 07:01 PM
[NMR paper] Segmental isotopic labeling for structural biological applications of NMR.
Segmental isotopic labeling for structural biological applications of NMR. Related Articles Segmental isotopic labeling for structural biological applications of NMR. Methods Mol Biol. 2004;278:47-56 Authors: Cowburn D, Shekhtman A, Xu R, Ottesen JJ, Muir TW This chapter describes the preparation of precursor domains for the formation of multidomain segmentally labeled proteins by protein ligation.
nmrlearner Journal club 0 11-24-2010 09:25 PM
[NMR paper] Chain-selective isotopic labeling for NMR studies of large multimeric proteins: appli
Chain-selective isotopic labeling for NMR studies of large multimeric proteins: application to hemoglobin. Related Articles Chain-selective isotopic labeling for NMR studies of large multimeric proteins: application to hemoglobin. Biophys J. 2000 Aug;79(2):1146-54 Authors: Simplaceanu V, Lukin JA, Fang TY, Zou M, Ho NT, Ho C Multidimensional, multinuclear NMR has the potential to elucidate the mechanisms of allostery and cooperativity in multimeric proteins under near-physiological conditions. However, NMR studies of proteins made up of...
nmrlearner Journal club 0 11-19-2010 08:29 PM
[NMR paper] Chemical ligation of folded recombinant proteins: segmental isotopic labeling of doma
Chemical ligation of folded recombinant proteins: segmental isotopic labeling of domains for NMR studies. Related Articles Chemical ligation of folded recombinant proteins: segmental isotopic labeling of domains for NMR studies. Proc Natl Acad Sci U S A. 1999 Jan 19;96(2):388-93 Authors: Xu R, Ayers B, Cowburn D, Muir TW A convenient in vitro chemical ligation strategy has been developed that allows folded recombinant proteins to be joined together. This strategy permits segmental, selective isotopic labeling of the product. The src homology...
nmrlearner Journal club 0 11-18-2010 07:05 PM
[NMR tweet] RT @IOP_NANO: Force-detected nuclear magnetic resonance: recent advances and future c
RT @IOP_NANO: Force-detected nuclear magnetic resonance: recent advances and future challenges http://bit.ly/db9hhF #nanotechnology Published by nanogrupo (Nanoscience) on 2010-11-11T13:21:27Z Source: Twitter
nmrlearner Twitter NMR 0 11-11-2010 01:34 PM
[NMR paper] Cell-free synthesis and amino acid-selective stable isotope labeling of proteins for
Cell-free synthesis and amino acid-selective stable isotope labeling of proteins for NMR analysis. Related Articles Cell-free synthesis and amino acid-selective stable isotope labeling of proteins for NMR analysis. J Biomol NMR. 1995 Sep;6(2):129-34 Authors: Kigawa T, Muto Y, Yokoyama S For the application of multidimensional NMR spectroscopy to larger proteins, it would be useful to perform selective labeling of one of the 20 amino acids. For some amino acids, however, amino acid metabolism drastically reduces the efficiency and selectivity...
nmrlearner Journal club 0 08-22-2010 03:50 AM
[NMR paper] Uniform 13C isotope labeling of proteins with sodium acetate for NMR studies: applica
Uniform 13C isotope labeling of proteins with sodium acetate for NMR studies: application to human carbonic anhydrase II. Related Articles Uniform 13C isotope labeling of proteins with sodium acetate for NMR studies: application to human carbonic anhydrase II. Biochemistry. 1991 May 7;30(18):4491-4 Authors: Venters RA, Calderone TL, Spicer LD, Fierke CA Uniform double labeling of proteins for NMR studies can be prohibitively expensive, even with an efficient expression and purification scheme, due largely to the high cost of glucose. We...
nmrlearner Journal club 0 08-21-2010 11:16 PM
A simple method for amino acid selective isotope labeling of recombinant proteins in E. coli
A simple method for amino acid selective isotope labeling of recombinant proteins in E. coli Kit I. Tong, Masayuki Yamamoto and Toshiyuki Tanaka Journal of Biomolecular NMR; 2008; 42(1); pp 59-67 Abstract: A simple and user-friendly method of labeling protein selectively with amino acids in vivo is introduced. This technique does not require the use of transaminase-deficient or auxotrophic strains. By manipulating the product feedback inhibitory loops of the E. coli amino acid metabolic pathways and, if necessary, by using enzyme inhibitors, proteins were labeled efficiently in vivo...
Brian Journal club 0 09-17-2008 10:20 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 - 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 05:02 AM.


Map