'Invisible' protein structure explains the power of enzymes - Phys.Org

		BioNMR > NMR community > Online News
'Invisible' protein structure explains the power of enzymes - 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

07-03-2015, 07:40 PM

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

'Invisible' protein structure explains the power of enzymes - Phys.Org

'Invisible' protein structure explains the power of enzymes - Phys.Org

Phys.Org

'Invisible' protein structure explains the power of enzymes
Phys.Org
The discovery has been made possible thanks to a broad scientific approach where numerous advanced biophysical techniques have been used; Nuclear Magnetic Resonance (NMR) and x-ray crystallography being the main techniques. "One of the ...

and more »
Read here

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
[NMR paper] Visualizing Side-chains of Invisible Protein Conformers by Solution NMR. Visualizing Side-chains of Invisible Protein Conformers by Solution NMR. Related Articles Visualizing Side-chains of Invisible Protein Conformers by Solution NMR. J Mol Biol. 2013 Nov 7; Authors: Bouvignies G, Vallurupalli P, Kay LE Abstract Sparsely populated and transiently formed protein conformers can play key roles in many biochemical processes. Understanding the structure function paradigm requires, therefore, an atomic resolution description of these rare states. Yet they are difficult to study because they cannot be observed using...	nmrlearner	Journal club	0	11-12-2013 03:52 PM
Visualizing Side-chains of Invisible Protein Conformers by Solution NMR Visualizing Side-chains of Invisible Protein Conformers by Solution NMR Publication date: Available online 8 November 2013 Source:Journal of Molecular Biology</br> Author(s): Guillaume Bouvignies , Pramodh Vallurupalli , Lewis E. Kay</br> Sparsely populated and transiently formed protein conformers can play key roles in many biochemical processes. Understanding the structure function paradigm requires, therefore, an atomic resolution description of these rare states. Yet they are difficult to study because they cannot be observed using standard biophysical...	nmrlearner	Journal club	0	11-08-2013 01:42 PM
3D structure of an unmodified G protein-coupled receptor in its natural habitat - Phys.Org 3D structure of an unmodified G protein-coupled receptor in its natural habitat - Phys.Org <img alt="" height="1" width="1" /> 3D structure of an unmodified G protein-coupled receptor in its natural habitat Phys.Org Using NMR spectroscopy, the team mapped the arrangement of atoms in a protein called CXCR1, which detects the inflammatory signal interleukin 8 and, through a G protein located inside the cell, triggers a cascade of events that can mobilize immune ... and more » Read here	nmrlearner	Online News	0	11-04-2012 05:53 AM
Crystal structure of a cyanobacterial protein associated with nitrogen fixation - Phys.Org Crystal structure of a cyanobacterial protein associated with nitrogen fixation - Phys.Org <img alt="" height="1" width="1" /> Crystal structure of a cyanobacterial protein associated with nitrogen fixation Phys.Org NMR and other biophysical data collected at EMSL confirmed that the biological unit of DUF269 in solution was the same as observed in the asymmetric unit of the crystal, a dimer. Further biochemical experiments are in progress to determine the ... Read here	nmrlearner	Online News	0	07-24-2012 08:28 PM
Wavelet transform analysis of NMR structure ensembles to reveal internal fluctuations of enzymes. Wavelet transform analysis of NMR structure ensembles to reveal internal fluctuations of enzymes. Wavelet transform analysis of NMR structure ensembles to reveal internal fluctuations of enzymes. Amino Acids. 2011 Apr 9; Authors: Hu M, Li Y, Yang G, Li G, Li M, Wen Z Internal motions and flexibility are essential for biological functions in proteins. To assess the internal fluctuations and conformational flexibility of proteins, reliable computational methods are needed. In this study, wavelet transformation was used to filter out the noise and...	nmrlearner	Journal club	0	04-12-2011 11:08 AM
Measuring 1HN temperature coefficients in invisible protein states by relaxation dispersion NMR spectroscopy Measuring 1HN temperature coefficients in invisible protein states by relaxation dispersion NMR spectroscopy Abstract A method based on the Carr-Purcell-Meiboom-Gill relaxation dispersion experiment is presented for measuring the temperature coefficients of amide proton chemical shifts of low populated â??invisibleâ?? protein states that exchange with a â??visibleâ?? ground state on the millisecond time-scale. The utility of the approach is demonstrated with an application to an I58D mutant of the Pfl6 Cro protein that undergoes exchange between the native, folded state and a cold...	nmrlearner	Journal club	0	03-22-2011 07:32 PM
Using relaxation dispersion NMR spectroscopy to determine structures of excited, invisible protein states Using relaxation dispersion NMR spectroscopy to determine structures of excited, invisible protein states D. Flemming Hansen, Pramodh Vallurupalli and Lewis E. Kay Journal of Biomolecular NMR; 2008; 41(3); pp 113 - 120 Abstract: Currently the main focus of structural biology is the determination of static three-dimensional representations of biomolecules that for the most part correspond to low energy (ground state) conformations. However, it is becoming increasingly well recognized that higher energy structures often play important roles in function as well. Because these conformers...	daniel	Journal club	0	08-03-2008 03:16 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