NMR tweet Hadamard NMR spectroscopy for relaxation measurements of large (>35 kDa) proteins

		BioNMR > NMR community > Twitter NMR
[NMR tweet] Hadamard NMR spectroscopy for relaxation measurements of large (>35 kDa) proteins

Webservers

NMR processing:

MDD

NMR assignment:

Backbone:

Side-chains:

NOEs:

Structure from NMR restraints:

Ab initio:

Fragment-based:

Rosetta-NMR (Robetta)

Template-based:

GeNMR

I-TASSER

Refinement:

Amber

Structure from chemical shifts:

Fragment-based:

Homology-based:

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:

NMR model quality:

NOEs, other restraints:

Chemical shifts:

RDCs:

Pseudocontact shifts:

Protein geomtery:

SAVES2 or SAVES4

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:

Isotope labeling:

Solid-state NMR:

Thread Tools

Search this Thread

Rate Thread

Display Modes

08-16-2010, 02:01 AM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,732

Points: 193,617, Level: 100

Level up: 0%, 0 Points needed

Activity: 50.7%

Last Achievements

Award-Showcase

NMR Credits: 0

NMR Points: 193,617

Downloads: 0

Uploads: 0

Nuclear magnetic resonance lipoprotein subclasses and the apoe genotype influence car

Nuclear magnetic resonance lipoprotein subclasses and the apoe genotype influence carotid atheroscler... http://bit.ly/cHYtEg #Rheumatology

Published by MDLinx (Sandeep Pulim MD) on 2010-08-16T07:24:44Z

Source: Twitter

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
Three-dimensional deuterium-carbon correlation experiments for high-resolution solid-state MAS NMR spectroscopy of large proteins Three-dimensional deuterium-carbon correlation experiments for high-resolution solid-state MAS NMR spectroscopy of large proteins Abstract Well-resolved 2Hâ??13C correlation spectra, reminiscent of 1Hâ??13C correlations, are obtained for perdeuterated ubiquitin and for perdeuterated outer-membrane protein G (OmpG) from E. coli by exploiting the favorable lifetime of 2H double-quantum (DQ) states. Sufficient signal-to-noise was achieved due to the short deuterium T 1, allowing for high repetition rates and enabling 3D experiments with a 2Hâ??13C transfer step in a reasonable time....	nmrlearner	Journal club	0	11-01-2011 01:52 AM
TROSY NMR Spectroscopy of Large Soluble Proteins. TROSY NMR Spectroscopy of Large Soluble Proteins. TROSY NMR Spectroscopy of Large Soluble Proteins. Top Curr Chem. 2011 Sep 17; Authors: Xu Y, Matthews S Abstract Solution nuclear magnetic resonance spectroscopy is usually only used to study proteins with molecular weight not exceeding about 50 kDa. This size limit has been lifted significantly in recent years, thanks to the development of labelling methods and the application of transverse-relaxation optimized spectroscopy (TROSY). In particular, methyl-specific labelling and...	nmrlearner	Journal club	0	09-20-2011 03:10 PM
Selective 1H-13C NMR spectroscopy of methyl groups in residually protonated samples of large proteins Selective 1H-13C NMR spectroscopy of methyl groups in residually protonated samples of large proteins Abstract Methyl 13CHD2 isotopomers of all methyl-containing amino-acids can be observed in residually protonated samples of large proteins obtained from -glucose/D2O-based bacterial media, with sensitivity sufficient for a number of NMR applications. Selective detection of some subsets of methyl groups (AlaÎ², ThrÎ³2) is possible using simple â??out-and-backâ?? NMR methodology. Such selective methyl-detected â??out-and-backâ?? NMR experiments allow complete assignments of threonine Î³2...	nmrlearner	Journal club	0	01-09-2011 12:46 PM
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...	nmrlearner	Journal club	0	01-09-2011 12:46 PM
[NMR paper] Relaxation-optimized NMR spectroscopy of methylene groups in proteins and nucleic aci Relaxation-optimized NMR spectroscopy of methylene groups in proteins and nucleic acids. Related Articles Relaxation-optimized NMR spectroscopy of methylene groups in proteins and nucleic acids. J Am Chem Soc. 2004 Sep 1;126(34):10560-70 Authors: Miclet E, Williams Jr DC, Clore GM, Bryce DL, Boisbouvier J, Bax A A large fraction of hydrogens in proteins and nucleic acids is of the methylene type. Their detailed study, however, in terms of structure and dynamics by NMR spectroscopy is hampered by their fast relaxation properties, which give...	nmrlearner	Journal club	0	11-24-2010 10:01 PM
[NMR paper] Practical methods for solid-state NMR distance measurements on large biomolecules: co Practical methods for solid-state NMR distance measurements on large biomolecules: constant-time rotational resonance. Related Articles Practical methods for solid-state NMR distance measurements on large biomolecules: constant-time rotational resonance. J Magn Reson. 1999 Aug;139(2):371-6 Authors: Balazs YS, Thompson LK Simple modifications of the rotational resonance experiment substantially reduce the total experimental time needed to measure weak homonuclear dipolar couplings, a critical factor for achieving routine internuclear distance...	nmrlearner	Journal club	0	11-18-2010 08:31 PM
[NMR paper] 3D NMR experiments for measuring 15N relaxation data of large proteins: application t 3D NMR experiments for measuring 15N relaxation data of large proteins: application to the 44 kDa ectodomain of SIV gp41. Related Articles 3D NMR experiments for measuring 15N relaxation data of large proteins: application to the 44 kDa ectodomain of SIV gp41. J Magn Reson. 1998 Dec;135(2):368-72 Authors: Caffrey M, Kaufman J, Stahl SJ, Wingfield PT, Gronenborn AM, Clore GM A suite of 3D NMR experiments for measuring 15N-¿1H¿ NOE, 15N T1, and 15N T1rho values in large proteins, uniformly labeled with 15N and 13C, is presented. These...	nmrlearner	Journal club	0	11-17-2010 11:15 PM
Hadamard NMR spectroscopy for relaxation measurements of large (>35 kDa) proteins Hadamard NMR spectroscopy for relaxation measurements of large (>35 kDa) proteins B. Tom Burnley, Arnout P. Kalverda, Stephen J. Paisey, Alan Berry and Steve W. Homans Journal of Biomolecular NMR; 2007; 39(3) pp 239 - 245 Abstract: Here we present a suite of pulse sequences for the measurement of 15N T1, T1ρ and NOE data that combine traditional TROSY-based pulse sequences with band-selective Hadamard frequency encoding. The additive nature of the Hadamard matrix produces much reduced resonance overlap without the need for an increase in the dimensionality of the experiment or a...	linawaed	Journal club	0	08-04-2008 10:43 AM

« Previous Thread | Next 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 Off Trackbacks are Off Pingbacks are Off Refbacks are Off