NMR paper A Positively Charged Liquid Crystalline Medium for Measuring Residual Dipolar Couplings in Membrane Proteins by NMR.

		BioNMR > Educational resources > Journal club
[NMR paper] A Positively Charged Liquid Crystalline Medium for Measuring Residual Dipolar Couplings in Membrane Proteins by NMR.

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:

View First Unread

Thread Tools

Search this Thread

Rate Thread

Display Modes

09-09-2015, 11:49 AM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,184

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

A Positively Charged Liquid Crystalline Medium for Measuring Residual Dipolar Couplings in Membrane Proteins by NMR.

A Positively Charged Liquid Crystalline Medium for Measuring Residual Dipolar Couplings in Membrane Proteins by NMR.

A Positively Charged Liquid Crystalline Medium for Measuring Residual Dipolar Couplings in Membrane Proteins by NMR.

J Am Chem Soc. 2015 Sep 8;

Authors: Thiagarajan-Rosenkranz Paltr Uic Edu P, Draney AW, Smrt ST, Lorieau JL

Abstract
Residual Dipolar Couplings (RDCs) are integral to the refinement of membrane protein structures by NMR since they accurately define the orientation of helices and other structural units. Only a small set of liquid crystals used for RDC measurements are compatible with the detergents needed in membrane protein studies. The available detergent-compatible liquid crystals are negatively charged, thus offering effectively only one of five orthogonal components of the alignment Saupe matrix. In this communication, we present a robust liquid crystalline medium that is positively charged, pinacyanol acetate (PNA), for the determination of orthogonal sets of RDCs in membrane. This new medium promises to enhance the accuracy of membrane protein structures and the measurement of dynamics based on RDCs.

PMID: 26348133 [PubMed - as supplied by publisher]

More...

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
[NMR paper] Solution NMR Experiment for Measurement of 15N-1H Residual Dipolar Couplings in Large Proteins and Supramolecular Complexes. Solution NMR Experiment for Measurement of 15N-1H Residual Dipolar Couplings in Large Proteins and Supramolecular Complexes. Related Articles Solution NMR Experiment for Measurement of 15N-1H Residual Dipolar Couplings in Large Proteins and Supramolecular Complexes. J Am Chem Soc. 2015 Aug 21; Authors: Eletsky A, Pulavarti SV, Beaumont V, Gollnick P, Szyperski T Abstract NMR residual dipolar couplings (RDCs) are exquisite probes of protein structure and dynamics. A new solution NMR experiment named 2D SE2 J-TROSY is presented to...	nmrlearner	Journal club	0	08-22-2015 11:20 AM
Determination of structural fluctuations of proteins from structure-based calculations of residual dipolar couplings Determination of structural fluctuations of proteins from structure-based calculations of residual dipolar couplings Abstract Residual dipolar couplings (RDCs) have the potential of providing detailed information about the conformational fluctuations of proteins. It is very challenging, however, to extract such information because of the complex relationship between RDCs and protein structures. A promising approach to decode this relationship involves structure-based calculations of the alignment tensors of protein conformations. By implementing this strategy to generate structural...	nmrlearner	Journal club	0	06-26-2012 06:18 AM
Simultaneous measurement of 1Hâ??15N and Methyl 1Hmâ??13Cm residual dipolar couplings in large proteins Simultaneous measurement of 1Hâ??15N and Methyl 1Hmâ??13Cm residual dipolar couplings in large proteins Abstract A two-dimensional TROSY-based SIM-13Cmâ??1Hm/1Hâ??15N NMR experiment for simultaneous measurements of methyl 1 D CH and backbone amide 1 D NH residual dipolar couplings (RDC) in {U-; IleÎ´1-; Leu,Val-}-labeled samples of large proteins is described. Significant variation in the alignment tensor of the 82-kDa enzyme Malate synthase G is observed as a function of only slight changes in experimental conditions. The SIM-13Cmâ??1Hm/1Hâ??15N data sets provide convenient means...	nmrlearner	Journal club	0	09-30-2011 08:01 PM
Rapid measurement of residual dipolar couplings for fast fold elucidation of proteins Rapid measurement of residual dipolar couplings for fast fold elucidation of proteins Abstract It has been demonstrated that protein folds can be determined using appropriate computational protocols with NMR chemical shifts as the sole source of experimental restraints. While such approaches are very promising they still suffer from low convergence resulting in long computation times to achieve accurate results. Here we present a suite of time- and sensitivity optimized NMR experiments for rapid measurement of up to six RDCs per residue. Including such an RDC data set, measured in less...	nmrlearner	Journal club	0	09-17-2011 10:20 AM
[NMR paper] NMR spectroscopy of proteins encapsulated in a positively charged surfactant. NMR spectroscopy of proteins encapsulated in a positively charged surfactant. Related Articles NMR spectroscopy of proteins encapsulated in a positively charged surfactant. J Magn Reson. 2005 Jul;175(1):158-62 Authors: Lefebvre BG, Liu W, Peterson RW, Valentine KG, Wand AJ Traditionally, large proteins, aggregation-prone proteins, and membrane proteins have been difficult to examine by modern multinuclear and multidimensional solution NMR spectroscopy. A major limitation presented by these protein systems is that their slow molecular...	nmrlearner	Journal club	0	11-25-2010 08:21 PM
[NMR paper] Controlling residual dipolar couplings in high-resolution NMR of proteins by strain i Controlling residual dipolar couplings in high-resolution NMR of proteins by strain induced alignment in a gel. Related Articles Controlling residual dipolar couplings in high-resolution NMR of proteins by strain induced alignment in a gel. J Biomol NMR. 2001 Oct;21(2):141-51 Authors: Ishii Y, Markus MA, Tycko R Water-soluble biological macromolecules can be weakly aligned by dissolution in a strained, hydrated gel such as cross-linked polyacrylamide, an effect termed 'strain-induced alignment in a gel' (SAG). SAG induces nonzero nuclear...	nmrlearner	Journal club	0	11-19-2010 08:44 PM
[NMR paper] Orienting domains in proteins using dipolar couplings measured by liquid-state NMR: d Orienting domains in proteins using dipolar couplings measured by liquid-state NMR: differences in solution and crystal forms of maltodextrin binding protein loaded with beta-cyclodextrin. Related Articles Orienting domains in proteins using dipolar couplings measured by liquid-state NMR: differences in solution and crystal forms of maltodextrin binding protein loaded with beta-cyclodextrin. J Mol Biol. 2000 Feb 4;295(5):1265-73 Authors: Skrynnikov NR, Goto NK, Yang D, Choy WY, Tolman JR, Mueller GA, Kay LE Protein function is often regulated...	nmrlearner	Journal club	0	11-18-2010 09:15 PM
Theoretical framework for NMR residual dipolar couplings in unfolded proteins Theoretical framework for NMR residual dipolar couplings in unfolded proteins O. I. Obolensky, Kai Schlepckow, Harald Schwalbe and A. V. Solov’yov Journal of Biomolecular NMR; 2007; 39(1) pp 1-16 Abstract: A theoretical framework for the prediction of nuclear magnetic resonance (NMR) residual dipolar couplings (RDCs) in unfolded proteins under weakly aligning conditions is presented. The unfolded polypeptide chain is modeled as a random flight chain while the alignment medium is represented by a set of regularly arranged obstacles. For the case of bicelles oriented perpendicular to...	stewart	Journal club	0	08-05-2008 02:26 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 On Trackbacks are Off Pingbacks are Off Refbacks are Off