Molecular trap allows study of single proteins - Phys.org

		BioNMR > NMR community > Online News
Molecular trap allows study of single proteins - Phys.org

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

11-27-2021, 09:42 AM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,191

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

Molecular trap allows study of single proteins - Phys.org

Molecular trap allows study of single proteins - Phys.org

Molecular trap allows study of single proteins Phys.org Read here

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
Researchers probe brain disease-causing proteins at the atomic level: A change in a single amino acid determines which species are vulnerable, study finds - Science Daily Researchers probe brain disease-causing proteins at the atomic level: A change in a single amino acid determines which species are vulnerable, study finds - Science Daily Researchers probe brain disease-causing proteins at the atomic level: A change in a single amino acid determines which species are vulnerable, study finds Science DailyResearchers studying a protein that causes a hereditary degenerative brain disease in humans have discovered that the human, mouse and hamster forms of ... Read here	nmrlearner	Online News	0	04-06-2019 06:58 PM
DNA damage repairâ??molecular insights - Phys.Org <img alt="" height="1" width="1"> DNA damage repairâ??molecular insights Phys.Org Using nuclear magnetic resonance spectroscopy, which allows for characterization of the structures of XPA molecules, they identified the critical parts of the protein that are responsible for binding DNA. Moreover, their results revealed that the ... DNA damage repairâ??molecular insights - Phys.Org More...	nmrlearner	Online News	0	12-08-2017 01:06 AM
Nanodiscs catch misfolding proteins red-handed - Phys.org - Phys.Org Nanodiscs catch misfolding proteins red-handed - Phys.org - Phys.Org <img alt="" height="1" width="1"> Nanodiscs catch misfolding proteins red-handed - Phys.org Phys.Org When proteins misfold, accumulate and clump around insulin-producing cells in the pancreas, they kill cells. Now, researchers, including University of Michigan biophysicists, have obtained a structural snapshot of these proteins ... and more » Read here	nmrlearner	Online News	0	12-06-2017 11:04 PM
New polymer allows researchers to study how proteins fold, function - Phys.Org http://www.bionmr.com//t1.gstatic.com/images?q=tbn:ANd9GcT1vCTGweCRCGnIIM-HRmhT9xDnnv3hykhpSgGt-WxcRQUrDustcGzFLfUfgIKl41L5goXKEV89 Phys.Org <img alt="" height="1" width="1"> New polymer allows researchers to study how proteins fold, function Phys.Org Researchers then use a technique called nuclear magnetic resonance imaging to image the protein at an atomic level within the nanodisc. These techniques are being developed in the Ramamoorthy lab to study the structures of an enzyme called cytochrome ... and more » New polymer allows researchers to study how proteins fold,...	nmrlearner	Online News	0	08-17-2017 12:56 AM
[NMR paper] CH3-specific NMR assignment of alanine, isoleucine, leucine and valine methyl groups in high molecular weight proteins using a single sample. CH3-specific NMR assignment of alanine, isoleucine, leucine and valine methyl groups in high molecular weight proteins using a single sample. Related Articles CH3-specific NMR assignment of alanine, isoleucine, leucine and valine methyl groups in high molecular weight proteins using a single sample. J Biomol NMR. 2015 Nov 13; Authors: Kerfah R, Hamelin O, Boisbouvier J, Marion D Abstract A new strategy for the NMR assignment of aliphatic side-chains in large perdeuterated proteins is proposed. It involves an alternative isotopic...	nmrlearner	Journal club	0	11-15-2015 07:55 PM
CH 3 -specific NMR assignment of alanine, isoleucine, leucine and valine methyl groups in high molecular weight proteins using a single sample CH 3 -specific NMR assignment of alanine, isoleucine, leucine and valine methyl groups in high molecular weight proteins using a single sample Abstract A new strategy for the NMR assignment of aliphatic side-chains in large perdeuterated proteins is proposed. It involves an alternative isotopic labeling protocol, the use of an out-and-back 13Câ??13C TOCSY experiment ((H)C-TOCSY-C-TOCSY-(C)H) and an optimized non-uniform sampling protocol. It has long been known that the non-linearity of an aliphatic spin-system (for example Ile, Val, or Leu)...	nmrlearner	Journal club	0	11-14-2015 03:37 PM
Waking proteins up from deep sleep to study their motions - Phys.Org Waking proteins up from deep sleep to study their motions - Phys.Org <img alt="" height="1" width="1"> Waking proteins up from deep sleep to study their motions Phys.Org In order to carry out their functions, proteins need to move. Scientists at EPFL have developed a new technique to study motions in proteins with unprecedented accuracy. The method, which is based on NMR, freezes proteins down to immobility, then ... Read here	nmrlearner	Online News	0	04-30-2015 09:13 PM
Methanol Strengthens Hydrogen Bonds and Weakens Hydrophobic Interactions in Proteins - A Combined Molecular Dynamics and NMR study. Methanol Strengthens Hydrogen Bonds and Weakens Hydrophobic Interactions in Proteins - A Combined Molecular Dynamics and NMR study. Methanol Strengthens Hydrogen Bonds and Weakens Hydrophobic Interactions in Proteins - A Combined Molecular Dynamics and NMR study. J Phys Chem B. 2011 May 2; Authors: Hwang S, Shao Q, Williams H, Hilty C, Gao YQ A combined simulation and experimental study was performed to investigate how methanol affects the structure of a model peptide BBA5. BBA5 forms a stable ?-hairpin-?-helix structure in aqueous solutions....	nmrlearner	Journal club	0	05-04-2011 04:14 PM

« 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