Catalytic site mutations confer multiple states of G protein activation - Science

		BioNMR > NMR community > Online News
Catalytic site mutations confer multiple states of G protein activation - Science

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

02-15-2023, 11:58 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

Catalytic site mutations confer multiple states of G protein activation - Science

Catalytic site mutations confer multiple states of G protein activation - Science

Catalytic site mutations confer multiple states of G protein activation Science Read here

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
Mutations linked to neurological disease enhance self-association of low-complexity protein sequences - Science Mutations linked to neurological disease enhance self-association of low-complexity protein sequences Science Mutations linked to neurological disease enhance self-association of low-complexity protein sequences - Science More...	nmrlearner	Online News	0	07-01-2022 10:59 AM
[NMR paper] Protein Yoga: Conformational Versatility of the Hemolysin II C-terminal Domain Detailed by NMR Structures for Multiple States Protein Yoga: Conformational Versatility of the Hemolysin II C-terminal Domain Detailed by NMR Structures for Multiple States The C-terminal domain of Bacillus cereus hemolysin II, HlyIIC, stabilizes the trans-membrane-pore formed by the HlyII toxin and may aid in target cell recognition. Initial efforts to determine the NMR structure of HlyIIC were hampered by cis/trans isomerization about the single proline at position 405, that leads to doubling of NMR resonances. We used the mutant P405M-HlyIIC that eliminates the cis proline to determine the NMR structure of the domain, which revealed...	nmrlearner	Journal club	0	03-20-2021 02:31 AM
Protein Yoga: Conformational Versatility of the Hemolysin II C-terminal Domain Detailed by NMR Structures for Multiple States Protein Yoga: Conformational Versatility of the Hemolysin II C-terminal Domain Detailed by NMR Structures for Multiple States ABSTRACT The C-terminal domain of Bacillus cereus hemolysin II, HlyIIC, stabilizes the trans-membrane-pore formed by the HlyII toxin and may aid in target cell recognition. Initial efforts to determine the NMR structure of HlyIIC were hampered by cis/trans isomerization about the single proline at position 405, that leads to doubling of NMR resonances. We used the mutant P405M-HlyIIC that eliminates the cis proline to determine the NMR structure of the domain,...	nmrlearner	Journal club	0	03-18-2021 05:17 PM
[ASAP] Protein–Ligand Interactions in the STING Binding Site Probed by Rationally Designed Single-Point Mutations: Experiment and Theory Protein–Ligand Interactions in the STING Binding Site Probed by Rationally Designed Single-Point Mutations: Experiment and Theory https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.0c00949/20210215/images/medium/bi0c00949_0007.gif Biochemistry DOI: 10.1021/acs.biochem.0c00949 http://feeds.feedburner.com/~r/acs/bichaw/~4/JqMF5MXiewc More...	nmrlearner	Journal club	0	02-18-2021 03:17 PM
[NMR paper] Bioorthogonal Catalytic Activation Of Pt And Ru Anticancer Complexes By FAD And Flavoproteins Bioorthogonal Catalytic Activation Of Pt And Ru Anticancer Complexes By FAD And Flavoproteins Recent advances in bioorthogonal catalysis promise to deliver new chemical tools for performing chemoselective transformations in complex biological environments. Herein we report how FAD (flavin adenine dinucleotide), FMN (flavin mononucleotide) and four flavoproteins behave as unconventional photocatalysts capable of converting PtIV and RuII complexes into potentially toxic PtII or RuII-OH2 species. Using electron donors and low doses of visible light, the flavoproteins mini Singlet Oxygen...	nmrlearner	Journal club	0	01-23-2018 03:50 PM
[NMR paper] NMR study of mutations of glycine-52 of the catalytic domain of diphtheria toxin. NMR study of mutations of glycine-52 of the catalytic domain of diphtheria toxin. NMR study of mutations of glycine-52 of the catalytic domain of diphtheria toxin. J Pharm Biomed Anal. 2017 Dec 02;150:72-79 Authors: Sauvé S, Gingras G, Aubin Y Abstract Cross-reacting-material 197 (CRM197) is a naturally occurring non-toxic mutant of diphtheria toxin (DT) that is one of the few carrier protein used in the manufacture of polysaccharide vaccines targeting bacterial pathogens such as Neisseria meningitidis, Streptococcus...	nmrlearner	Journal club	0	12-08-2017 02:25 PM
Study shows how mutations disrupt ALS-linked protein - Science Codex <img alt="" height="1" width="1"> Study shows how mutations disrupt ALS-linked protein Science Codex Using nuclear magnetic resonance, computer simulations and microscopy, Fawzi, Brown graduate student Alexander Conicella and colleagues at Lehigh University were able to show that under normal circumstances, TDP-43 molecules concentrate into little ... Study shows how mutations disrupt ALS-linked protein - Science Codex More...	nmrlearner	Online News	0	08-19-2016 05:49 PM
Persistent Activation of cGMP-Dependent Protein Kinaseby a Nitrated Cyclic Nucleotide via Site Specific Protein S-Guanylation Persistent Activation of cGMP-Dependent Protein Kinaseby a Nitrated Cyclic Nucleotide via Site Specific Protein S-Guanylation http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.5b00774/20160129/images/medium/bi-2015-00774n_0003.gif Biochemistry DOI: 10.1021/acs.biochem.5b00774 http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/bichaw/~4/KLjU9u3Nnwk More...	nmrlearner	Journal club	0	01-30-2016 07:56 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