NMR structures of two designed proteins with high sequence identity but different fold and function - pnas.org

		BioNMR > NMR community > Online News
NMR structures of two designed proteins with high sequence identity but different fold and function - pnas.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

09-07-2024, 02:30 PM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,596

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 structures of two designed proteins with high sequence identity but different fold and function - pnas.org

NMR structures of two designed proteins with high sequence identity but different fold and function - pnas.org

NMR structures of two designed proteins with high sequence identity but different fold and function pnas.org Read here

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
Exploiting conformational dynamics to modulate the function of designed proteins \| Proceedings of the National ... - pnas.org Exploiting conformational dynamics to modulate the function of designed proteins \| Proceedings of the National ... - pnas.org Exploiting conformational dynamics to modulate the function of designed proteins \| Proceedings of the National ... pnas.org Read here	nmrlearner	Online News	0	12-13-2023 02:17 PM
Exploiting conformational dynamics to modulate the function of designed proteins \| Proceedings of the National ... - pnas.org Exploiting conformational dynamics to modulate the function of designed proteins \| Proceedings of the National ... - pnas.org Exploiting conformational dynamics to modulate the function of designed proteins \| Proceedings of the National ... pnas.org Read here	nmrlearner	Online News	0	12-13-2023 02:17 PM
Study reveals evolutionary origins of fold-switching protein - pnas.org Study reveals evolutionary origins of fold-switching protein - pnas.org Study reveals evolutionary origins of fold-switching protein pnas.org Read here	nmrlearner	Online News	0	12-06-2023 02:55 AM
[NMR paper] AI-designed NMR spectroscopy RF pulses for fast acquisition at high and ultra-high magnetic fields AI-designed NMR spectroscopy RF pulses for fast acquisition at high and ultra-high magnetic fields Nuclear magnetic resonance (NMR) spectroscopy is a powerful high-resolution tool for characterizing biomacromolecular structure, dynamics, and interactions. However, the lengthy longitudinal relaxation of the nuclear spins significantly extends the total experimental time, especially at high and ultra-high magnetic field strengths. Although longitudinal relaxation-enhanced techniques have sped up data acquisition, their application has been limited by the chemical shift dispersion. Here we......	nmrlearner	Journal club	0	07-14-2023 07:47 PM
De novo designed protein inhibitors of amyloid aggregation and seeding \| Proceedings of the National Academy of Sciences - pnas.org De novo designed protein inhibitors of amyloid aggregation and seeding \| Proceedings of the National Academy of Sciences - pnas.org De novo designed protein inhibitors of amyloid aggregation and seeding \| Proceedings of the National Academy of Sciences pnas.org Read here	nmrlearner	Online News	0	08-24-2022 02:40 PM
Study reveals evolutionary origins of fold-switching protein - pnas.org Study reveals evolutionary origins of fold-switching protein pnas.org Study reveals evolutionary origins of fold-switching protein - pnas.org More...	nmrlearner	Online News	0	01-15-2021 04:25 PM
New polymer allows researchers to study how proteins fold, function - Phys.Org http://www.bionmr.com//t1.gstatic.com/images?q=tbn:ANd9GcT1vCTGweCRCGnIIM-HRmhT9xDnnv3hykhpSgGt-WxcRQUrDustcGzFLfUfgIKl41L5goXKEV89 Phys.Org <img alt="" height="1" width="1"> New polymer allows researchers to study how proteins fold, function Phys.Org Researchers then use a technique called nuclear magnetic resonance imaging to image the protein at an atomic level within the nanodisc. These techniques are being developed in the Ramamoorthy lab to study the structures of an enzyme called cytochrome ... and more » New polymer allows researchers to study how proteins fold,...	nmrlearner	Online News	0	08-17-2017 12:56 AM
[NMR paper] NMR hydrogen exchange of the OB-fold protein LysN as a function of denaturant: the mo NMR hydrogen exchange of the OB-fold protein LysN as a function of denaturant: the most conserved elements of structure are the most stable to unfolding. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR hydrogen exchange of the OB-fold protein LysN as a function of denaturant: the most conserved elements of structure are the most stable to unfolding. J Mol Biol. 1999 Jun 18;289(4):1041-54 Authors: Alexandrescu AT, Jaravine VA, Dames SA, Lamour FP The structure of...	nmrlearner	Journal club	0	08-21-2010 04:03 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