NMR paper Quantifying Siglec-sialylated ligand interactions: a versatile (19)F-T(2) CPMG filtered competitive NMR displacement assay

		BioNMR > Educational resources > Journal club
[NMR paper] Quantifying Siglec-sialylated ligand interactions: a versatile (19)F-T(2) CPMG filtered competitive NMR displacement assay

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

07-12-2024, 11:00 AM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,574

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

Quantifying Siglec-sialylated ligand interactions: a versatile (19)F-T(2) CPMG filtered competitive NMR displacement assay

Quantifying Siglec-sialylated ligand interactions: a versatile (19)F-T(2) CPMG filtered competitive NMR displacement assay

Sialic-acid-binding immunoglobulin-like lectins (Siglecs) are integral cell surface proteins crucial for the regulation of immune responses and the maintenance of immune tolerance through interactions with sialic acids. Siglecs recognize sialic acid moieties, usually found at the end of N-glycan and O-glycan chains. However, the different Siglecs prefer diverse presentations of the recognized sialic acid, depending on the type of glycosidic linkage used to link to the contiguous Gal/GalNAc or...

More...

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
[NMR paper] Estimating the cooperativity of PROTAC-induced ternary complexes using (19)F NMR displacement assay Estimating the cooperativity of PROTAC-induced ternary complexes using (19)F NMR displacement assay Cooperativity is an important parameter to understand the ternary complexes formed by protein degraders. We developed fluorine NMR competition binding experiments to determine cooperativity of PROTACs. We show applicability to estimate both positive and negative cooperativity, also with homo-dimerizers, and highlight key features and considerations for optimal assay development. More...	nmrlearner	Journal club	0	11-17-2021 07:58 AM
[NMR paper] NMR waterLOGSY as An Assay in Drug Development Programmes for Detecting Protein-Ligand Interactions-NMR waterLOGSY NMR waterLOGSY as An Assay in Drug Development Programmes for Detecting Protein-Ligand Interactions-NMR waterLOGSY In drug development programmes, multiple assays are needed for the determination of protein-compound interactions and evaluation of potential use in assays with protein-protein interactions. In this protocol we describe the waterLOGSY NMR method for confirming protein-ligand binding events. More...	nmrlearner	Journal club	0	03-04-2021 12:41 PM
[NMR paper] Quantifying Millisecond Exchange Dynamics in Proteins by CPMG Relaxation Dispersion NMR Using Side-Chain (1)H Probes. From Mendeley Biomolecular NMR group: Quantifying Millisecond Exchange Dynamics in Proteins by CPMG Relaxation Dispersion NMR Using Side-Chain (1)H Probes. Journal of the American Chemical Society (2012). Volume: 134, Issue: 6. Pages: 3178-3189. Alexandar L Hansen, Patrik Lundström, Algirdas Velyvis, Lewis E Kay et al. A Carr-Purcell-Meiboom-Gill relaxation dispersion experiment is presented for quantifying millisecond time-scale chemical exchange at side-chain (1)H positions in proteins. Such experiments are not possible in a fully protonated molecule because of magnetization...	nmrlearner	Journal club	0	10-17-2013 12:49 PM
[NMR paper] Quantifying Millisecond Exchange Dynamics in Proteins by CPMG Relaxation Dispersion NMR Using Side-Chain (1)H Probes. From Mendeley Biomolecular NMR group: Quantifying Millisecond Exchange Dynamics in Proteins by CPMG Relaxation Dispersion NMR Using Side-Chain (1)H Probes. Journal of the American Chemical Society (2012). Volume: 134, Issue: 6. Pages: 3178-3189. Alexandar L Hansen, Patrik Lundström, Algirdas Velyvis, Lewis E Kay et al. A Carr-Purcell-Meiboom-Gill relaxation dispersion experiment is presented for quantifying millisecond time-scale chemical exchange at side-chain (1)H positions in proteins. Such experiments are not possible in a fully protonated molecule because of magnetization...	nmrlearner	Journal club	0	01-02-2013 01:48 PM
[NMR paper] Quantifying Millisecond Exchange Dynamics in Proteins by CPMG Relaxation Dispersion NMR Using Side-Chain (1)H Probes. From Mendeley Biomolecular NMR group: Quantifying Millisecond Exchange Dynamics in Proteins by CPMG Relaxation Dispersion NMR Using Side-Chain (1)H Probes. Journal of the American Chemical Society (2012). Volume: 134, Issue: 6. Pages: 3178-3189. Alexandar L Hansen, Patrik Lundström, Algirdas Velyvis, Lewis E Kay et al. A Carr-Purcell-Meiboom-Gill relaxation dispersion experiment is presented for quantifying millisecond time-scale chemical exchange at side-chain (1)H positions in proteins. Such experiments are not possible in a fully protonated molecule because of magnetization...	nmrlearner	Journal club	0	11-22-2012 11:49 AM
[NMR paper] Quantifying Millisecond Exchange Dynamics in Proteins by CPMG Relaxation Dispersion NMR Using Side-Chain (1)H Probes. From Mendeley Biomolecular NMR group: Quantifying Millisecond Exchange Dynamics in Proteins by CPMG Relaxation Dispersion NMR Using Side-Chain (1)H Probes. Journal of the American Chemical Society (2012). Volume: 134, Issue: 6. Pages: 3178-3189. Alexandar L Hansen, Patrik Lundström, Algirdas Velyvis, Lewis E Kay et al. A Carr-Purcell-Meiboom-Gill relaxation dispersion experiment is presented for quantifying millisecond time-scale chemical exchange at side-chain (1)H positions in proteins. Such experiments are not possible in a fully protonated molecule because of magnetization...	nmrlearner	Journal club	0	10-12-2012 09:58 AM
[NMR paper] Quantifying Millisecond Exchange Dynamics in Proteins by CPMG Relaxation Dispersion NMR Using Side-Chain (1)H Probes. From Mendeley Biomolecular NMR group: Quantifying Millisecond Exchange Dynamics in Proteins by CPMG Relaxation Dispersion NMR Using Side-Chain (1)H Probes. Journal of the American Chemical Society (2012). Volume: 134, Issue: 6. Pages: 3178-3189. Alexandar L Hansen, Patrik Lundström, Algirdas Velyvis, Lewis E Kay et al. A Carr-Purcell-Meiboom-Gill relaxation dispersion experiment is presented for quantifying millisecond time-scale chemical exchange at side-chain (1)H positions in proteins. Such experiments are not possible in a fully protonated molecule because of magnetization...	nmrlearner	Journal club	0	08-24-2012 08:01 PM
Quantifying Millisecond Exchange Dynamics in Proteins by CPMG Relaxation Dispersion NMR Using Side-Chain 1H Probes Quantifying Millisecond Exchange Dynamics in Proteins by CPMG Relaxation Dispersion NMR Using Side-Chain 1H Probes Alexandar L. Hansen, Patrik Lundstrom, Algirdas Velyvis and Lewis E. Kay http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja210711v/aop/images/medium/ja-2011-10711v_0008.gif Journal of the American Chemical Society DOI: 10.1021/ja210711v http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/jacsat/~4/jaMjjnA_QTw	nmrlearner	Journal club	0	02-03-2012 09:50 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