A direct nuclear magnetic resonance method to investigate lysine acetylation of intrinsically disordered proteins - Frontiers

		BioNMR > NMR community > Online News
A direct nuclear magnetic resonance method to investigate lysine acetylation of intrinsically disordered proteins - Frontiers

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

07-27-2023, 10:14 PM

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

A direct nuclear magnetic resonance method to investigate lysine acetylation of intrinsically disordered proteins - Frontiers

A direct nuclear magnetic resonance method to investigate lysine acetylation of intrinsically disordered proteins Frontiers
A direct nuclear magnetic resonance method to investigate lysine acetylation of intrinsically disordered proteins - Frontiers
More...

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
Using NMR to investigate intrinsically disordered proteins: an interview with Dr Isabella Felli - News-Medical.net Using NMR to investigate intrinsically disordered proteins: an interview with Dr Isabella Felli - News-Medical.net Using NMR to investigate intrinsically disordered proteins: an interview with Dr Isabella Felli News-Medical.netIDPs” is now a widely used acronym that stands for “intrinsically disordered proteins.” It is the term generally used by the scientific community to refer to a wide ... Read here	nmrlearner	Online News	0	04-05-2019 08:33 AM
Using NMR to investigate intrinsically disordered proteins: an interview with Dr Isabella Felli - News-Medical.net Using NMR to investigate intrinsically disordered proteins: an interview with Dr Isabella Felli - News-Medical.net Using NMR to investigate intrinsically disordered proteins: an interview with Dr Isabella Felli News-Medical.netIDPs” is now a widely used acronym that stands for “intrinsically disordered proteins.” It is the term generally used by the scientific community to refer to a wide ... Read here	nmrlearner	Online News	0	01-07-2019 05:49 AM
[NMR paper] Direct Detection of Carbon and Nitrogen Nuclei for High-Resolution Analysis of Intrinsically Disordered Proteins using NMR Spectroscopy. Direct Detection of Carbon and Nitrogen Nuclei for High-Resolution Analysis of Intrinsically Disordered Proteins using NMR Spectroscopy. Direct Detection of Carbon and Nitrogen Nuclei for High-Resolution Analysis of Intrinsically Disordered Proteins using NMR Spectroscopy. Methods. 2018 Jan 13;: Authors: Gibbs EB, Kriwacki RW Abstract Nuclear magnetic resonance spectroscopy (NMR) is a powerful technique for characterizing the structural and dynamic properties of intrinsically disordered proteins and protein regions (IDPs &...	nmrlearner	Journal club	0	01-18-2018 12:41 PM
Direct Detection of Carbon and Nitrogen Nuclei for High-Resolution Analysis of Intrinsically Disordered Proteins using NMR Spectroscopy Direct Detection of Carbon and Nitrogen Nuclei for High-Resolution Analysis of Intrinsically Disordered Proteins using NMR Spectroscopy Publication date: Available online 16 January 2018 Source:Methods</br> Author(s): E.B. Gibbs, R.W. Kriwacki</br> Nuclear magnetic resonance spectroscopy (NMR) is a powerful technique for characterizing the structural and dynamic properties of intrinsically disordered proteins and protein regions (IDPs & IDRs). However, the application of NMR to IDPs has been limited by poor chemical shift dispersion in two-dimensional (2D) 1H-15N...	nmrlearner	Journal club	0	01-17-2018 07:00 PM
Using NMR to investigate intrinsically disordered proteins: an interview with Dr Isabella Felli - News-Medical.net Using NMR to investigate intrinsically disordered proteins: an interview with Dr Isabella Felli - News-Medical.net <img alt="" height="1" width="1"> Using NMR to investigate intrinsically disordered proteins: an interview with Dr Isabella Felli News-Medical.net This mainstream understanding kept the scientific community distracted from also focusing on a lot of other important proteins, such as the more flexible ones. We all know how NMR spectroscopy is not only used to look at structural information, but can ... and more » Read here	nmrlearner	Online News	0	07-01-2016 03:06 AM
[NMR paper] Longitudinal relaxation properties of (1)H(N) and (1)H(?) determined by direct-detected (13)C NMR experiments to study intrinsically disordered proteins (IDPs). Longitudinal relaxation properties of (1)H(N) and (1)H(?) determined by direct-detected (13)C NMR experiments to study intrinsically disordered proteins (IDPs). Longitudinal relaxation properties of (1)H(N) and (1)H(?) determined by direct-detected (13)C NMR experiments to study intrinsically disordered proteins (IDPs). J Magn Reson. 2015 Feb 12;254:19-26 Authors: Hošek T, Gil-Caballero S, Pierattelli R, Brutscher B, Felli IC Abstract Intrinsically disordered proteins (IDPs) are functional proteins containing large...	nmrlearner	Journal club	0	03-17-2015 05:12 PM
Longitudinal relaxation properties of 1HN and 1H? determined by direct-detected 13C NMR experiments to study intrinsically disordered proteins (IDPs) Longitudinal relaxation properties of 1HN and 1H? determined by direct-detected 13C NMR experiments to study intrinsically disordered proteins (IDPs) Publication date: Available online 12 February 2015 Source:Journal of Magnetic Resonance</br> Author(s): Tomáš Hošek , Sergi Gil-Caballero , Roberta Pierattelli , Bernhard Brutscher , Isabella C. Felli</br> Intrinsically disordered proteins (IDPs) are functional proteins containing large fragments characterized by high local mobility. Bioinformatic studies have suggested that a significant fraction (more than 30%)...	nmrlearner	Journal club	0	02-12-2015 07:48 PM
[NMR paper] High-dimensionality (13)C direct-detected NMR experiments for the automatic assignment of intrinsically disordered proteins. High-dimensionality (13)C direct-detected NMR experiments for the automatic assignment of intrinsically disordered proteins. Related Articles High-dimensionality (13)C direct-detected NMR experiments for the automatic assignment of intrinsically disordered proteins. J Biomol NMR. 2013 Nov 8; Authors: Bermel W, Felli IC, Gonnelli L, Ko?mi?ski W, Piai A, Pierattelli R, Zawadzka-Kazimierczuk A Abstract We present three novel exclusively heteronuclear 5D (13)C direct-detected NMR experiments, namely (H(N-flip)N)CONCACON, (HCA)CONCACON and...	nmrlearner	Journal club	0	11-11-2013 01:30 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