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

Go Back   BioNMR > Educational resources > Conferences
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  
Unread 05-23-2006, 09:39 AM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,175
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

Wheat Germ Cell-Free Protein Production Workshop


PDF file


The Center for Eukaryotic Structural Genomics (CESG) and the Nuclear Magnetic Resonance Facility at Madison
(NMRFAM) are pleased to announce the first Wheat Germ Cell-Free Protein Production Workshop to be held from
July 30 - August 4, 2006, at the Department of Biochemistry at the University of Wisconsin-Madison in Madison, Wisconsin,
USA. To register for this workshop, complete the Registration Form on the next page and mail in with your NONREFUNDABLE
payment of $500.00 (academic) or $750.00 (private industry) by May 15, 2006.

PURPOSE
The workshop will offer participants a unique opportunity to obtain hands-on experience with cell-free protein production
from wheat germ extracts. The week-long workshop will cover various aspects of small-scale expression screening (μg
quantities of attendee-nominated target protein) and large-scale production (mg quantities of target protein selected from
attendee efforts) of labeled proteins for NMR spectroscopy or crystallization screening. Both manual and automated
procedures will be covered.

SCOPE
Participants can try these approaches with their own targets. Necessary protocols will be sent to all participants just prior to
the workshop. All the data generated during the workshop by all of the participants as well as any relevant presentation and
seminar materials will be sent to all of the participants after the completion of the workshop. The workshop will be limited to
24 participants and geared toward scientists with at least 3-5 years of experience in protein production and purification. A
registration fee will be required to help defray reagent costs.

TRAVEL AND LODGING
Travel and lodging need be arranged by each participant. We have a block of rooms set aside that you can reserve for a
reduced rate ($89 for one person or $99 for two people per night) at the Best Western InnTowner (www.inntowner.com).
When you make your reservation, ask for a room in the "CESG block." NOTE: This block of rooms will only be available
until June 1, 2006. This hotel was chosen because it is very convenient to CESG and NMRFAM. They have a free shuttle
which will bring you right to the workshop location, or one can walk the distance in about 15 minutes.

REGISTRATION
Your registration fee of $500.00 (academic) or $750.00 (private industry) includes the workshop fees, dinner at the opening and
closing receptions, and continental breakfast, lunch buffets, and afternoon breaks every day. The preferred method for payment of
your registration fee is by credit card, but can also be made in U.S. funds, drawn on a U.S. bank, or by international money order
payable to "University of Wisconsin-Madison." Your registration fee is NON-REFUNDABLE, and the registration deadline for the
workshop is May 15, 2006. Participation in the workshop will be limited to a total of 24 participants, so we encourage those
who are interested to register early. Instructional materials (protocols, links to reference information, and data) will be sent
to participants in advance of the workshop. If you have any questions, send an e-mail to: cesginfo@biochem.wisc.edu.
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
Erratum to: Suppression of isotope scrambling in cell-free protein synthesis by broadband inhibition of PLP enymes for selective 15N-labelling and production of perdeuterated proteins in H2O
Erratum to: Suppression of isotope scrambling in cell-free protein synthesis by broadband inhibition of PLP enymes for selective 15N-labelling and production of perdeuterated proteins in H2O Erratum to: Suppression of isotope scrambling in cell-free protein synthesis by broadband inhibition of PLP enymes for selective 15N-labelling and production of perdeuterated proteins in H2O Content Type Journal Article Category Erratum Pages 1-1 DOI 10.1007/s10858-011-9562-9 Authors
nmrlearner Journal club 0 09-20-2011 05:02 AM
Suppression of isotope scrambling in cell-free protein synthesis by broadband inhibition of PLP enymes for selective 15N-labelling and production of perdeuterated proteins in H2O
Suppression of isotope scrambling in cell-free protein synthesis by broadband inhibition of PLP enymes for selective 15N-labelling and production of perdeuterated proteins in H2O Abstract Selectively isotope labelled protein samples can be prepared in vivo or in vitro from selectively labelled amino acids but, in many cases, metabolic conversions between different amino acids result in isotope scrambling. The best results are obtained by cell-free protein synthesis, where metabolic enzymes are generally less active, but isotope scrambling can never be suppressed completely. We show that...
nmrlearner Journal club 0 02-16-2011 09:34 PM
[NMR paper] Cell-free protein synthesis in an autoinduction system for NMR studies of protein-protein interactions.
Cell-free protein synthesis in an autoinduction system for NMR studies of protein-protein interactions. Related Articles Cell-free protein synthesis in an autoinduction system for NMR studies of protein-protein interactions. J Biomol NMR. 2005 Jul;32(3):235-41 Authors: Ozawa K, Jergic S, Crowther JA, Thompson PR, Wijffels G, Otting G, Dixon NA Cell-free protein synthesis systems provide facile access to proteins in a nascent state that enables formation of soluble, native protein-protein complexes even if one of the protein components is prone...
nmrlearner Journal club 0 12-01-2010 06:56 PM
[NMR paper] Quantitation of protein expression in a cell-free system: Efficient detection of yiel
Quantitation of protein expression in a cell-free system: Efficient detection of yields and 19F NMR to identify folded protein. Related Articles Quantitation of protein expression in a cell-free system: Efficient detection of yields and 19F NMR to identify folded protein. J Biomol NMR. 2005 Jan;31(1):11-9 Authors: Neerathilingam M, Greene LH, Colebrooke SA, Campbell ID, Staunton D We have developed an efficient and novel filter assay method, involving radioactive labelling and imaging, to quantify the expression of soluble proteins from a...
nmrlearner Journal club 0 11-24-2010 11:14 PM
[NMR paper] Cell-free protein production and labeling protocol for NMR-based structural proteomic
Cell-free protein production and labeling protocol for NMR-based structural proteomics. Related Articles Cell-free protein production and labeling protocol for NMR-based structural proteomics. Nat Methods. 2004 Nov;1(2):149-53 Authors: Vinarov DA, Lytle BL, Peterson FC, Tyler EM, Volkman BF, Markley JL Structural proteomics requires robust, scalable methods. Here we describe a wheat germ cell-free platform for protein production that supports efficient NMR structural studies of eukaryotic proteins and offers advantages over cell-based methods....
nmrlearner Journal club 0 11-24-2010 10:01 PM
[NMR paper] NMR and molecular modeling studies of the interaction between wheat germ agglutinin a
NMR and molecular modeling studies of the interaction between wheat germ agglutinin and the beta-D-GlcpNAc-(1-->6)-alpha-D-Manp epitope present in glycoproteins of tumor cells. Related Articles NMR and molecular modeling studies of the interaction between wheat germ agglutinin and the beta-D-GlcpNAc-(1-->6)-alpha-D-Manp epitope present in glycoproteins of tumor cells. Biochemistry. 2004 Aug 3;43(30):9647-54 Authors: Lycknert K, Edblad M, Imberty A, Widmalm G The beta-D-GlcpNAc-(1-->6)-alpha-D-Manp disaccharide is a constituent of highly...
nmrlearner Journal club 0 11-24-2010 10:01 PM
[NMR paper] 13C NMR studies of wheat germ agglutinin interactions with N-acetylglucosamine at a m
13C NMR studies of wheat germ agglutinin interactions with N-acetylglucosamine at a magnetically oriented bilayer surface. Related Articles 13C NMR studies of wheat germ agglutinin interactions with N-acetylglucosamine at a magnetically oriented bilayer surface. Biochemistry. 1994 Aug 23;33(33):10137-48 Authors: Hare BJ, Rise F, Aubin Y, Prestegard JH The orientation of synthetic 13C-labeled glycolipid receptors and their interaction with the plant lectin wheat germ agglutinin have been studied in an oriented membrane system using NMR...
nmrlearner Journal club 0 08-22-2010 03:29 AM
Cell-free protein synthesis of perdeuterated proteins for NMR studies
Cell-free protein synthesis of perdeuterated proteins for NMR studies Touraj Etezady-Esfarjani, Sebastian Hiller, Cristina Villalba and Kurt Wüthrich Journal of Biomolecular NMR; 2007; 39(3); pp 229-238 Abstract: Cell-free protein synthesis protocols for uniformly deuterated proteins typically yield low, non-uniform deuteration levels. This paper introduces an E. coli cell-extract, D-S30, which enables efficient production of proteins with high deuteration levels for all non-labile hydrogen atom positions. Potential applications of the new protocol may include production of proteins...
Deano Journal club 0 08-14-2008 10:01 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 02:20 PM.


Map