B2LiVe, a label-free 1D-NMR method to quantify the binding of amphitropic peptides or proteins to membrane vesicles - ScienceDirect

		BioNMR > NMR community > Online News
B2LiVe, a label-free 1D-NMR method to quantify the binding of amphitropic peptides or proteins to membrane vesicles - ScienceDirect

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:

View First Unread

Thread Tools

Search this Thread

Rate Thread

Display Modes

12-28-2023, 10:50 PM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,192

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

B2LiVe, a label-free 1D-NMR method to quantify the binding of amphitropic peptides or proteins to membrane vesicles - ScienceDirect

B2LiVe, a label-free 1D-NMR method to quantify the binding of amphitropic peptides or proteins to membrane vesicles - ScienceDirect

B2LiVe, a label-free 1D-NMR method to quantify the binding of amphitropic peptides or proteins to membrane vesicles ScienceDirect Read here

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
[NMR paper] B2LiVe, a label-free 1D-NMR method to quantify the binding of amphitropic peptides or proteins to membrane vesicles B2LiVe, a label-free 1D-NMR method to quantify the binding of amphitropic peptides or proteins to membrane vesicles Amphitropic proteins and peptides reversibly partition from solution to membrane, a key process that regulates their functions. Experimental approaches classically used to measure protein partitioning into lipid bilayers, such as fluorescence and circular dichroism, are hardly usable when the peptides or proteins do not exhibit significant polarity and/or conformational changes upon membrane binding. Here, we describe binding to lipid vesicles (B2LiVe), a simple, robust, and...	nmrlearner	Journal club	0	11-01-2023 03:27 PM
[NMR paper] High-Precision Mapping of Membrane Proteins on Synaptic Vesicles using Spectrally Encoded Super-Resolution Imaging High-Precision Mapping of Membrane Proteins on Synaptic Vesicles using Spectrally Encoded Super-Resolution Imaging Angewandte Chemie International Edition, Accepted Article. More...	nmrlearner	Journal club	0	01-01-2023 02:41 AM
[ASAP] High-Resolution In Situ NMR Spectroscopy of Bacterial Envelope Proteins in Outer Membrane Vesicles High-Resolution In Situ NMR Spectroscopy of Bacterial Envelope Proteins in Outer Membrane Vesicles https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.9b01123/20200406/images/medium/bi9b01123_0004.gif Biochemistry DOI: 10.1021/acs.biochem.9b01123 http://feeds.feedburner.com/~r/acs/bichaw/~4/2_SiKyocUYc More...	nmrlearner	Journal club	0	04-07-2020 07:35 PM
[NMR paper] High-resolution in-situ NMR spectroscopy of bacterial envelope proteins in outer membrane vesicles. High-resolution in-situ NMR spectroscopy of bacterial envelope proteins in outer membrane vesicles. http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles High-resolution in-situ NMR spectroscopy of bacterial envelope proteins in outer membrane vesicles. Biochemistry. 2020 Apr 01;: Authors: Thoma J, Burmann BM Abstract The cell envelope of Gram-negative bacteria is an elaborate cellular environment, consisting of two lipid membranes separated by the aqueous...	nmrlearner	Journal club	0	04-03-2020 09:41 PM
[NMR paper] Binding mode of AIF(370-394) peptide to CypA: insights from NMR, label-free and molecular docking studies. Binding mode of AIF(370-394) peptide to CypA: insights from NMR, label-free and molecular docking studies. Related Articles Binding mode of AIF(370-394) peptide to CypA: insights from NMR, label-free and molecular docking studies. Biochem J. 2018 Jun 11;: Authors: Farina B, Sturlese M, Mascanzoni F, Caporale A, Monti A, Di Sorbo G, Fattorusso R, Ruvo M, Doti N Abstract The complex formation between the proteins Apoptosis Inducing Factor (AIF) and Cyclophilin A (CypA) following oxidative stress in neuronal cells has been suggested...	nmrlearner	Journal club	0	06-13-2018 05:09 PM
Topologically Diverse Human Membrane Proteins Partitionto Liquid-Disordered Domains in Phase-Separated Lipid Vesicles Topologically Diverse Human Membrane Proteins Partitionto Liquid-Disordered Domains in Phase-Separated Lipid Vesicles http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.5b01154/20160210/images/medium/bi-2015-01154x_0003.gif Biochemistry DOI: 10.1021/acs.biochem.5b01154 http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/bichaw/~4/FqvhNKDI0Xk More...	nmrlearner	Journal club	0	02-11-2016 10:30 PM
REDOR solid-state NMR as a probe of the membrane locations of membrane-associated peptides and proteins REDOR solid-state NMR as a probe of the membrane locations of membrane-associated peptides and proteins Publication date: April 2015 Source:Journal of Magnetic Resonance, Volume 253</br> Author(s): Lihui Jia , Shuang Liang , Kelly Sackett , Li Xie , Ujjayini Ghosh , David P. Weliky</br> Rotational-echo double-resonance (REDOR) solid-state NMR is applied to probe the membrane locations of specific residues of membrane proteins. Couplings are measured between protein 13CO nuclei and membrane lipid or cholesterol 2H and 31P nuclei. Specific 13CO labeling is used...	nmrlearner	Journal club	0	03-20-2015 01:48 AM
[Question from NMRWiki Q&A forum] When to label peptides and proteins and when not? When to label peptides and proteins and when not? When pursuing an NMR structure project - at what size of oligopeptide you would decide to label it with: 15N 13C both	nmrlearner	News from other NMR forums	0	08-22-2010 02:30 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