An introduction to NMR-based approaches for measuring protein dynamics - ScienceDirect.com

		BioNMR > NMR community > Online News
An introduction to NMR-based approaches for measuring protein dynamics - ScienceDirect.com

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

05-11-2024, 09:24 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

An introduction to NMR-based approaches for measuring protein dynamics - ScienceDirect.com

An introduction to NMR-based approaches for measuring protein dynamics - ScienceDirect.com

An introduction to NMR-based approaches for measuring protein dynamics ScienceDirect.com Read here

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
Review NMR-based investigation into protein phosphorylation - ScienceDirect.com Review NMR-based investigation into protein phosphorylation - ScienceDirect.com Review NMR-based investigation into protein phosphorylation ScienceDirect.com Read here	nmrlearner	Online News	0	02-25-2024 06:10 AM
NMR approaches for structural analysis of multidomain proteins and complexes in solution - ScienceDirect.com NMR approaches for structural analysis of multidomain proteins and complexes in solution - ScienceDirect.com NMR approaches for structural analysis of multidomain proteins and complexes in solution ScienceDirect.com Read here	nmrlearner	Online News	0	02-23-2024 09:09 AM
Cobalt-based paramagnetic probe to study RNA-protein interactions by NMR - ScienceDirect Cobalt-based paramagnetic probe to study RNA-protein interactions by NMR - ScienceDirect Cobalt-based paramagnetic probe to study RNA-protein interactions by NMR ScienceDirect Read here	nmrlearner	Online News	0	01-27-2024 01:53 PM
[NMR paper] Integrative approaches for characterizing protein dynamics: NMR, CryoEM, and computer simulations Integrative approaches for characterizing protein dynamics: NMR, CryoEM, and computer simulations Proteins are inherently dynamic and their internal motions are essential for biological function. Protein motions cover a broad range of timescales: 10^(-14)-10 s, spanning from sub-picosecond vibrational motions of atoms via microsecond loop conformational rearrangements to millisecond large amplitude domain reorientations. Observing protein dynamics over all timescales and connecting motions and structure to biological mechanisms requires integration of multiple experimental and...	nmrlearner	Journal club	0	12-05-2023 11:45 AM
[NMR paper] Convergent Views on Disordered Protein Dynamics From NMR and Computational Approaches Convergent Views on Disordered Protein Dynamics From NMR and Computational Approaches Intrinsically disordered proteins (IDPs) or intrinsically disordered regions (IDR) is a class of biologically important proteins exhibiting specific biophysical characteristics. They lack a hydrophobic core and their conformational behavior is strongly influenced by electrostatic interactions. IDPs and IDRs are highly dynamic and a characterization of the motions of IDPs and IDRs is essential for their physically correct description. Nuclear magnetic resonance (NMR) together with molecular... More...	nmrlearner	Journal club	0	09-23-2022 06:24 AM
[NMR paper] NMR-Based Approaches for the Identification and Optimization of Inhibitors of Protein-Protein Interactions. NMR-Based Approaches for the Identification and Optimization of Inhibitors of Protein-Protein Interactions. Related Articles NMR-Based Approaches for the Identification and Optimization of Inhibitors of Protein-Protein Interactions. Chem Rev. 2014 Apr 8; Authors: Barile E, Pellecchia M PMID: 24712885	nmrlearner	Journal club	0	04-10-2014 02:25 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
An introduction to NMR-based approaches for measuring protein dynamics. An introduction to NMR-based approaches for measuring protein dynamics. An introduction to NMR-based approaches for measuring protein dynamics. Biochim Biophys Acta. 2010 Nov 5; Authors: Kleckner IR, Foster MP Proteins are inherently flexible at ambient temperature. At equilibrium, they are characterized by a set of conformations that undergo continuous exchange within a hierarchy of spatial and temporal scales ranging from nanometers to micrometers and femtoseconds to hours. Dynamic properties of proteins are essential for describing the...	nmrlearner	Journal club	0	11-10-2010 02:29 PM

« 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