Waking proteins up from deep sleep to study their motions - Phys.Org

		BioNMR > NMR community > Online News
Waking proteins up from deep sleep to study their motions - Phys.Org

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

04-30-2015, 09:13 PM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,780

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

Waking proteins up from deep sleep to study their motions - Phys.Org

Waking proteins up from deep sleep to study their motions - Phys.Org

Waking proteins up from deep sleep to study their motions
Phys.Org
In order to carry out their functions, proteins need to move. Scientists at EPFL have developed a new technique to study motions in proteins with unprecedented accuracy. The method, which is based on NMR, freezes proteins down to immobility, then ...

Read here

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
Quantum Criticality in life's proteins - Phys.Org Quantum Criticality in life's proteins - Phys.Org http://www.bionmr.com//t0.gstatic.com/images?q=tbn:ANd9GcQmmwn4be-zSvmVia_TPrZnP9wSO0Vi4PWFRAoab1bWQiR7ZtGMlOjrGOQYnjAJsceK0vyZcMEu Phys.Org <img alt="" height="1" width="1"> Quantum Criticality in life's proteins Phys.Org In particular, they selected NMR spectra from the Protein Data Bank and used a technique known as the extended Huckel Hamiltonion method to calculate HOMO/LUMO orbitals for the proteins. For more comments on HOMO/LUMO orbital calculations you ...	nmrlearner	Online News	0	04-13-2015 09:11 PM
Proteins' passing phases revealed - Phys.Org <img alt="" height="1" width="1" /> Proteins' passing phases revealed Phys.Org X-ray crystallography and, more recently, nuclear magnetic resonance spectroscopy are the most common tools to see how the amino acids in a protein chain arrange themselves based on their attractive and repulsive energies, but they say nothing about ... Proteins' passing phases revealed - Phys.Org More...	nmrlearner	Online News	0	12-05-2013 06:57 PM
Erratic proteins: New insights into a transport mechanism - Phys.Org <img alt="" height="1" width="1" /> Erratic proteins: New insights into a transport mechanism Phys.Org "Only through employing modern nuclear magnetic resonance spectroscopy, it has become possible to detect this dynamic behavior within Skp." Transporting the membrane protein in such a changing state does not require energy and allows for its rapid ... Erratic proteins: New insights into a transport mechanism - Phys.Org More...	nmrlearner	Online News	0	09-30-2013 03:48 PM
New analysis shows how proteins shift into working mode - Phys.Org <img alt="" height="1" width="1" /> New analysis shows how proteins shift into working mode Phys.Org For more than 50 years, scientists around the world have combined experimental techniques such as X-ray crystallography and nuclear magnetic resonance imaging with computer algorithms to determine the three-dimensional structure of proteins. New analysis shows how proteins shift into working mode - Phys.Org More...	nmrlearner	Online News	0	08-09-2013 08:00 PM
A trick to fold proteins more quickly - PhysOrg.com - Phys.Org <img alt="" height="1" width="1" /> A trick to fold proteins more quickly - PhysOrg.com Phys.Org "We exploit the experimental data obtained observing the proteins through nuclear magnetic resonance, and use them to create restraints to be applied to the model", explained Laio, who has coordinated the research published in Proceedings of the ... A trick to fold proteins more quickly - PhysOrg.com - Phys.Org More...	nmrlearner	Online News	0	05-08-2013 02:49 PM
Intrinsically disordered proteins: A conversation with Rohit Pappu - Phys.Org Intrinsically disordered proteins: A conversation with Rohit Pappu - Phys.Org <img alt="" height="1" width="1" /> Intrinsically disordered proteins: A conversation with Rohit Pappu Phys.Org The earliest clue was that some protein segments didn't show up in X-ray crystallography or NMR studies, the standard ways of studying protein structure. By the 1990s people who studied how proteins interact with DNA had noticed the proteins often ... and more » Read here	nmrlearner	Online News	0	09-20-2012 06:36 PM
Speeding up drug discovery with rapid 3-D mapping of proteins - Phys.Org <img alt="" height="1" width="1" /> Speeding up drug discovery with rapid 3-D mapping of proteins Phys.Org These amino acids gave off telltale structural clues when analyzed with nuclear magnetic resonance spectroscopy, a method for using the magnetic properties of atoms to determine a molecule's physical and chemical properties. "It was very difficult and ... and more » Speeding up drug discovery with rapid 3-D mapping of proteins - Phys.Org More...	nmrlearner	Online News	0	05-30-2012 03:00 PM
[NMR paper] High pressure nmr study of dihydrofolate reductase from a deep-sea bacterium Moritell High pressure nmr study of dihydrofolate reductase from a deep-sea bacterium Moritella profunda. Related Articles High pressure nmr study of dihydrofolate reductase from a deep-sea bacterium Moritella profunda. Cell Mol Biol (Noisy-le-grand). 2004 Jun;50(4):311-6 Authors: Hata K, Kono R, Fujisawa M, Kitahara R, Kamatari YO, Akasaka K, Xu Y We have investigated the effect of pressure and temperature on the structural and thermodynamic stability of a protein dihydrofolate reductase from a deep-sea bacterium Moritella profunda in its folate-bound...	nmrlearner	Journal club	0	11-24-2010 09:51 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