Study of protein folding under native conditions by rapidly switching the hydrostatic pressure inside an NMR sample cell [Biophysics and Computational Biology]

		BioNMR > Educational resources > Journal club
Study of protein folding under native conditions by rapidly switching the hydrostatic pressure inside an NMR sample cell [Biophysics and Computational Biology]

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

05-01-2018, 10:57 PM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,819

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

Study of protein folding under native conditions by rapidly switching the hydrostatic pressure inside an NMR sample cell [Biophysics and Computational Biology]

Study of protein folding under native conditions by rapidly switching the hydrostatic pressure inside an NMR sample cell [Biophysics and Computational Biology]

Cyril Charlier, T. Reid Alderson, Joseph M. Courtney, Jinfa Ying, Philip Anfinrud, Adriaan Bax...
Date: 2018-05-01

In general, small proteins rapidly fold on the timescale of milliseconds or less. For proteins with a substantial volume difference between the folded and unfolded states, their thermodynamic equilibrium can be altered by varying the hydrostatic pressure. Using a pressure-sensitized mutant of ubiquitin, we demonstrate that rapidly switching the pressure... Read More

PNAS:
Number: 18
Volume: 115

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
[NMR paper] Study of protein folding under native conditions by rapidly switching the hydrostatic pressure inside an NMR sample cell. Study of protein folding under native conditions by rapidly switching the hydrostatic pressure inside an NMR sample cell. Related Articles Study of protein folding under native conditions by rapidly switching the hydrostatic pressure inside an NMR sample cell. Proc Natl Acad Sci U S A. 2018 Apr 16;: Authors: Charlier C, Alderson TR, Courtney JM, Ying J, Anfinrud P, Bax A Abstract In general, small proteins rapidly fold on the timescale of milliseconds or less. For proteins with a substantial volume difference between the folded...	nmrlearner	Journal club	0	04-19-2018 01:52 PM
Combining DNP NMR with segmental and specific labeling to study a yeast prion protein strain that is not parallel in-register [Biophysics and Computational Biology] Combining DNP NMR with segmental and specific labeling to study a yeast prion protein strain that is not parallel in-register Kendra K. Frederick, Vladimir K. Michaelis, Marc A. Caporini, Loren B. Andreas, Galia T. Debelouchina, Robert G. Griffin, Susan Lindquist... Date: 2017-04-04 The yeast prion protein Sup35NM is a self-propagating amyloid. Despite intense study, there is no consensus on the organization of monomers within Sup35NM fibrils. Some studies point to a ?-helical arrangement, whereas others suggest a parallel in-register organization. Intermolecular contacts are often...	nmrlearner	Journal club	0	04-04-2017 10:41 PM
Cavities and Cooperativity in the Folding of the Leucine Rich Repeat Protein PP32: A Pressure-Jump Fluorescence and High Pressure NMR Study Cavities and Cooperativity in the Folding of the Leucine Rich Repeat Protein PP32: A Pressure-Jump Fluorescence and High Pressure NMR Study Publication date: 3 February 2017 Source:Biophysical Journal, Volume 112, Issue 3, Supplement 1</br> Author(s): Kelly A. Jenkins, Martin Fossat, Thuy Dao, Yi Zhang, Zackery White, Doug Barrick, Catherine A. Royer</br> </br></br> </br></br> More...	nmrlearner	Journal club	0	02-03-2017 09:55 PM
Fluorine-19 NMR and computational quantification of isoflurane binding to the voltage-gated sodium channel NaChBac [Biophysics and Computational Biology] Fluorine-19 NMR and computational quantification of isoflurane binding to the voltage-gated sodium channel NaChBac Monica N. Kinde, Vasyl Bondarenko, Daniele Granata, Weiming Bu, Kimberly C. Grasty, Patrick J. Loll, Vincenzo Carnevale, Michael L. Klein, Roderic G. Eckenhoff, Pei Tang, Yan Xu... Date: 2016-11-29 Voltage-gated sodium channels (NaV) play an important role in general anesthesia. Electrophysiology measurements suggest that volatile anesthetics such as isoflurane inhibit NaV by stabilizing the inactivated state or altering the inactivation kinetics. Recent computational...	nmrlearner	Journal club	0	11-29-2016 09:02 PM
Protein NMR structures at >=100-kHz MAS [Biophysics and Computational Biology] Protein NMR structures at >=100-kHz MAS Andreas, L. B., Jaudzems, K., Stanek, J., Lalli, D., Bertarello, A., Le Marchand, T., Cala-De Paepe, D., Kotelovica, S., Akopjana, I., Knott, B., Wegner, S., Engelke, F., Lesage, A., Emsley, L., Tars, K., Herrmann, T., Pintacuda, G.... Date: 2016-08-16 Protein structure determination by proton-detected magic-angle spinning (MAS) NMR has focused on highly deuterated samples, in which only a small number of protons are introduced and observation of signals from side chains is extremely limited. Here, we show in two fully protonated proteins that,...	nmrlearner	Journal club	0	08-16-2016 07:38 PM
Protein dynamics from X-ray and NMR [Biophysics and Computational Biology] Protein dynamics from X-ray and NMR Fenwick, R. B., van den Bedem, H., Fraser, J. S., Wright, P. E.... Date: 2014-01-28 Detailed descriptions of atomic coordinates and motions are required for an understanding of protein dynamics and their relation to molecular recognition, catalytic function, and allostery. Historically, NMR relaxation measurements have played a dominant role in the determination of the amplitudes and timescales (picosecond–nanosecond) of bond vector fluctuations, whereas high-resolution X-ray... Read More PNAS: Number: 4	nmrlearner	Journal club	0	01-29-2014 12:50 AM
[NMR paper] Impact of Hydrostatic Pressure on an Intrinsically Disordered Protein: A High-Pressure NMR Study of ?-Synuclein. Impact of Hydrostatic Pressure on an Intrinsically Disordered Protein: A High-Pressure NMR Study of ?-Synuclein. Related Articles Impact of Hydrostatic Pressure on an Intrinsically Disordered Protein: A High-Pressure NMR Study of ?-Synuclein. Chembiochem. 2013 Jun 28; Authors: Roche J, Ying J, Maltsev AS, Bax A Abstract The impact of pressure on the backbone (15) N, (1) H and (13) C chemical shifts in N-terminally acetylated ?-synuclein has been evaluated over a pressure range 1-2500 bar. Even while the chemical shifts fall very close...	nmrlearner	Journal club	0	07-03-2013 01:46 PM
NMR and functional study of eIF4E3 [Biophysics and Computational Biology] NMR and functional study of eIF4E3 Osborne, M. J., Volpon, L., Kornblatt, J. A., Culjkovic-Kraljacic, B., Baguet, A., Borden, K. L. B.... Date: 2013-03-05 Recognition of the methyl-7-guanosine (m7G) cap structure on mRNA is an essential feature of mRNA metabolism and thus gene expression. Eukaryotic translation initiation factor 4E (eIF4E) promotes translation, mRNA export, proliferation, and oncogenic transformation dependent on this cap-binding activity. eIF4E–cap recognition is mediated via complementary charge interactions of the positively... Read More PNAS: Number: 10	nmrlearner	Journal club	0	03-06-2013 04:21 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