Fluorescence-activating beta-barrel protein made from scratch for first time - Phys.org

		BioNMR > NMR community > Online News
Fluorescence-activating beta-barrel protein made from scratch for first time - 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

01-07-2019, 05:49 AM

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

Fluorescence-activating beta-barrel protein made from scratch for first time - Phys.org

Fluorescence-activating beta-barrel protein made from scratch for first time - Phys.org

Fluorescence-activating beta-barrel protein made from scratch for first time Phys.orgFor the first time, scientists have created, entirely from scratch, a protein capable of binding to a small target molecule. Researchers from the University of ...

Read here

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
Nanodiscs catch misfolding proteins red-handed - Phys.org - Phys.Org Nanodiscs catch misfolding proteins red-handed - Phys.org - Phys.Org <img alt="" height="1" width="1"> Nanodiscs catch misfolding proteins red-handed - Phys.org Phys.Org When proteins misfold, accumulate and clump around insulin-producing cells in the pancreas, they kill cells. Now, researchers, including University of Michigan biophysicists, have obtained a structural snapshot of these proteins ... and more » Read here	nmrlearner	Online News	0	12-06-2017 11:04 PM
[NMR paper] A Pyrene-linked Cavity within a ?-Barrel Protein Promotes an Asymmetric Diels-Alder Reaction A Pyrene-linked Cavity within a ?-Barrel Protein Promotes an Asymmetric Diels-Alder Reaction A unique ?-expanded reaction cavity tethering a polycyclic moiety which provides a platform for substrate binding was constructed within the robust ?-barrel structure of nitrobindin (NB). NB variants with the cavities of different sizes and shapes are coupled with N-(1-pyrenyl)maleimide (Pyr) to prepare a series of NB-Pyr conjugates. The orientation of the pyrene moiety is fixed within the cavity by the coupling reaction. The fluorescent quenching analysis of NB-Pyr indicates that azachalcone...	nmrlearner	Journal club	0	08-10-2017 12:13 AM
Caught before Released: Structural Mapping of the Reaction Trajectory for the Sofosbuvir Activating Enzyme, Human Histidine Triad Nucleotide Binding Protein 1 (hHint1) Caught before Released: Structural Mapping of the Reaction Trajectory for the Sofosbuvir Activating Enzyme, Human Histidine Triad Nucleotide Binding Protein 1 (hHint1) http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00148/20170710/images/medium/bi-2017-00148s_0009.gif Biochemistry DOI: 10.1021/acs.biochem.7b00148 http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/bichaw/~4/SyXct7vdHtA More...	nmrlearner	Journal club	0	07-11-2017 09:20 AM
Light microscopy provides a deep look into protein structure - Phys.org - Phys.Org Light microscopy provides a deep look into protein structure - Phys.org - Phys.Org http://www.bionmr.com//t2.gstatic.com/images?q=tbn:ANd9GcQG69FMdjaOzVdvO8fNDx9c1t6uv0SeGKAywKjRdVRRma0SZH4sGlq9-_q3JW8xkTHitn6biYqD Phys.Org <img alt="" height="1" width="1"> Light microscopy provides a deep look into protein structure - Phys.org Phys.Org Light microscopy continues to reveal the microscopic world at an ever increasing resolution. Using a new method coined COLD, scientists at the Max Planck ... and more »	nmrlearner	Online News	0	01-25-2017 11:13 PM
[NMR paper] Lipid bilayer-bound conformation of an integral membrane beta barrel protein by multidimensional MAS NMR. Lipid bilayer-bound conformation of an integral membrane beta barrel protein by multidimensional MAS NMR. Related Articles Lipid bilayer-bound conformation of an integral membrane beta barrel protein by multidimensional MAS NMR. J Biomol NMR. 2015 Jan 30; Authors: Eddy MT, Su Y, Silvers R, Andreas L, Clark L, Wagner G, Pintacuda G, Emsley L, Griffin RG Abstract	nmrlearner	Journal club	0	01-31-2015 04:16 PM
Lipid bilayer-bound conformation of an integral membrane beta barrel protein by multidimensional MAS NMR Lipid bilayer-bound conformation of an integral membrane beta barrel protein by multidimensional MAS NMR Abstract The human voltage dependent anion channel 1 (VDAC) is a 32Â*kDa Î²-barrel integral membrane protein that controls the transport of ions across the outer mitochondrial membrane. Despite the determination of VDAC solution and diffraction structures, a structural basis for the mechanism of its function is not yet fully understood. Biophysical studies suggest VDAC requires a lipid bilayer to achieve full function, motivating the need...	nmrlearner	Journal club	0	01-30-2015 12:15 PM
[NMR paper] An NMR view of the unfolding process of rusticyanin: Structural elements that maintain the architecture of a beta-barrel metalloprotein. An NMR view of the unfolding process of rusticyanin: Structural elements that maintain the architecture of a beta-barrel metalloprotein. Related Articles An NMR view of the unfolding process of rusticyanin: Structural elements that maintain the architecture of a beta-barrel metalloprotein. Protein Sci. 2005 Jul;14(7):1710-22 Authors: Alcaraz LA, Jiménez B, Moratal JM, Donaire A The unfolding process of the blue copper protein rusticyanin (Rc) as well as its dynamic and D(2)O/H(2)O exchange properties in an incipient unfolded state have been...	nmrlearner	Journal club	0	12-01-2010 06:56 PM
[NMR paper] Folding of a beta-sheet protein monitored by real-time NMR spectroscopy. Folding of a beta-sheet protein monitored by real-time NMR spectroscopy. Related Articles Folding of a beta-sheet protein monitored by real-time NMR spectroscopy. J Mol Biol. 2003 May 16;328(5):1161-71 Authors: Mizuguchi M, Kroon GJ, Wright PE, Dyson HJ At low ionic strength, apoplastocyanin forms an unfolded state under non-denaturing conditions. The refolding of this state is sufficiently slow to allow real-time NMR experiments to be performed. Folding of apoplastocyanin, initiated by the addition of salt and followed by real-time 2D 1H-15N...	nmrlearner	Journal club	0	11-24-2010 09:01 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