NMR: The technique of choice for studying protein dynamics - SelectScience

		BioNMR > NMR community > Online News
NMR: The technique of choice for studying protein dynamics - SelectScience

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

03-21-2020, 03:13 PM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,777

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

NMR: The technique of choice for studying protein dynamics - SelectScience

NMR: The technique of choice for studying protein dynamics - SelectScience

NMR: The technique of choice for studying protein dynamics SelectScience Read here

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
[U. of Ottawa NMR Facility Blog] Appropriate Choice of Presaturation Time Appropriate Choice of Presaturation Time Presaturation is one of the most common methods of solvent suppression. A long selective low power pulse is applied at the solvent frequency followed by a hard non-selective read pulse (or composite pulse). Aside from a well-shimmed homogeneous magnet, there are two important parameters required for effective presaturation: saturation power and saturation time. The selection of saturation power was addressed in a previous post. With a properly selected saturation power, the appropriate choice for the saturation time depends on the relaxation...	nmrlearner	News from NMR blogs	0	03-29-2018 05:39 AM
[NMR paper] Studying Dynamics by Magic-Angle Spinning Solid-State NMR Spectroscopy: Principles and Applications to Biomolecules. Studying Dynamics by Magic-Angle Spinning Solid-State NMR Spectroscopy: Principles and Applications to Biomolecules. Studying Dynamics by Magic-Angle Spinning Solid-State NMR Spectroscopy: Principles and Applications to Biomolecules. Prog Nucl Magn Reson Spectrosc. 2016 Aug;96:1-46 Authors: Schanda P, Ernst M Abstract Magic-angle spinning solid-state NMR spectroscopy is an important technique to study molecular structure, dynamics and interactions, and is rapidly gaining importance in biomolecular sciences. Here we provide an...	nmrlearner	Journal club	0	04-26-2016 12:14 PM
Studying dynamics by magic-angle spinning solid-state NMR spectroscopy: Principles and applications to biomolecules Studying dynamics by magic-angle spinning solid-state NMR spectroscopy: Principles and applications to biomolecules Publication date: August 2016 Source:Progress in Nuclear Magnetic Resonance Spectroscopy, Volume 96</br> Author(s): Paul Schanda, Matthias Ernst</br> Magic-angle spinning solid-state NMR spectroscopy is an important technique to study molecular structure, dynamics and interactions, and is rapidly gaining importance in biomolecular sciences. Here we provide an overview of experimental approaches to study molecular dynamics by MAS solid-state NMR,...	nmrlearner	Journal club	0	04-09-2016 03:54 AM
[Question from NMRWiki Q&A forum] Choice of relaxation delay time (d1) in 2D experiments. Choice of relaxation delay time (d1) in 2D experiments. Hi, Most people tend to use a lower d1 for 2D than for 1D. Help me understand why. Furthermore, supposing you know your T1 value, what do you think is the "best" (or most effective while having the shortest experiment time) value for d1 in a 2D experiment? I'm not even sure my question makes any sense.	nmrlearner	News from other NMR forums	0	02-18-2015 06:15 PM
[NMR paper] Protein dynamics elucidated by NMR technique. Protein dynamics elucidated by NMR technique. http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Protein dynamics elucidated by NMR technique. Protein Cell. 2013 Oct;4(10):726-730 Authors: Li C, Tang C, Liu M PMID: 24104391	nmrlearner	Journal club	0	10-10-2013 09:38 PM
Computational approaches to the interpretation of NMR data for studying protein dynamics Computational approaches to the interpretation of NMR data for studying protein dynamics 2 March 2012 Publication year: 2012 Source:Chemical Physics, Volume 396</br> </br> Experimental studies of protein structure and dynamics with NMR provide the classical example of the power of theoretical approaches for the interpretation of experimental results. In this paper we review recent developments in experimental techniques extending the applicability of NMR to the study of protein structure and motion, and advances in the theoretical description. Graphical abstract ...	nmrlearner	Journal club	0	02-03-2013 10:13 AM
[NMR paper] General framework for studying the dynamics of folded and nonfolded proteins by NMR r General framework for studying the dynamics of folded and nonfolded proteins by NMR relaxation spectroscopy and MD simulation. Related Articles General framework for studying the dynamics of folded and nonfolded proteins by NMR relaxation spectroscopy and MD simulation. J Am Chem Soc. 2002 Apr 24;124(16):4522-34 Authors: Prompers JJ, Brüschweiler R A general framework is presented for the interpretation of NMR relaxation data of proteins. The method, termed isotropic reorientational eigenmode dynamics (iRED), relies on a principal component...	nmrlearner	Journal club	0	11-24-2010 08:49 PM
2H NMR Spin Relaxation for studying RNA dynamics A Suite of 2H NMR Spin Relaxation Experiments for the Measurement of RNA Dynamics Pramodh Vallurupalli and Lewis E. Kay, J. Am. Chem. Soc.; 2005; 127 (18) pp 6893 - 6901 ABSTRACT: A suite of (2)H-based spin relaxation NMR experiments is presented for the measurement of molecular dynamics in a site-specific manner in uniformly (13)C, randomly fractionally deuterated ( approximately 50%) RNA molecules. The experiments quantify (2)H R(1) and R(2) relaxation rates that can subsequently be analyzed to obtain information about dynamics on a pico- to nanosecond time scale. Sensitivity...	nmrlearner	Journal club	0	05-19-2005 08:44 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