Heredity matters: Ancestral protease functions as protein import motor in chloroplasts - Phys.org

		BioNMR > NMR community > Online News
Heredity matters: Ancestral protease functions as protein import motor in chloroplasts - 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:

Thread Tools

Search this Thread

Rate Thread

Display Modes

01-07-2019, 05:49 AM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,779

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

Heredity matters: Ancestral protease functions as protein import motor in chloroplasts - Phys.org

Heredity matters: Ancestral protease functions as protein import motor in chloroplasts - Phys.org

Heredity matters: Ancestral protease functions as protein import motor in chloroplasts Phys.orgOver 1 billion years ago, a relationship began between the ancestor of all living plants and a type of bacterium that paved the way for the evolution of life as we ...

Read here

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
[NMR paper] Segmental isotope labelling and solid-state NMR of a 12 × 59kDa motor protein: identification of structural variability. Segmental isotope labelling and solid-state NMR of a 12 × 59kDa motor protein: identification of structural variability. Related Articles Segmental isotope labelling and solid-state NMR of a 12 × 59*kDa motor protein: identification of structural variability. J Biomol NMR. 2018 Jun 12;: Authors: Wiegand T, Cadalbert R, von Schroetter C, Allain FH, Meier BH Abstract Segmental isotope labelling enables the NMR study of an individual domain within a multidomain protein, but still in the context of the entire full-length protein....	nmrlearner	Journal club	0	06-28-2018 02:38 PM
[NMR paper] Protein-nucleotide contacts in motor proteins detected by DNP-enhanced solid-state NMR. Protein-nucleotide contacts in motor proteins detected by DNP-enhanced solid-state NMR. Related Articles Protein-nucleotide contacts in motor proteins detected by DNP-enhanced solid-state NMR. J Biomol NMR. 2017 Nov 08;: Authors: Wiegand T, Liao WC, Ong TC, Däpp A, Cadalbert R, Copéret C, Böckmann A, Meier BH Abstract DNP (dynamic nuclear polarization)-enhanced solid-state NMR is employed to directly detect protein-DNA and protein-ATP interactions and identify the residue type establishing the intermolecular contacts. While...	nmrlearner	Journal club	0	11-10-2017 05:01 PM
Light microscopy provides a deep look into protein structure - Phys.org - Phys.Org Light microscopy provides a deep look into protein structure - Phys.org - Phys.Org http://www.bionmr.com//t2.gstatic.com/images?q=tbn:ANd9GcQG69FMdjaOzVdvO8fNDx9c1t6uv0SeGKAywKjRdVRRma0SZH4sGlq9-_q3JW8xkTHitn6biYqD Phys.Org <img alt="" height="1" width="1"> Light microscopy provides a deep look into protein structure - Phys.org Phys.Org Light microscopy continues to reveal the microscopic world at an ever increasing resolution. Using a new method coined COLD, scientists at the Max Planck ... and more »	nmrlearner	Online News	0	01-25-2017 11:13 PM
Translocator Protein 18 kDa (TSPO): An Old Proteinwith New Functions? Translocator Protein 18 kDa (TSPO): An Old Proteinwith New Functions? http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00142/20160509/images/medium/bi-2016-00142k_0009.gif Biochemistry DOI: 10.1021/acs.biochem.6b00142 http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/bichaw/~4/l_8dplFAYho More...	nmrlearner	Journal club	0	05-10-2016 04:13 AM
Selective observation of the disordered import signal of a globular protein by in-cell NMR: The example of frataxins Selective observation of the disordered import signal of a globular protein by in-cell NMR: The example of frataxins Abstract We have exploited the capability of in-cell NMR to selectively observe flexible regions within folded proteins to carry out a comparative study of two members of the highly conserved frataxin family which are found both in prokaryotes and in eukaryotes. They all contain a globular domain which shares more than 50% identity, which in eukaryotes is preceded by an N-terminal tail containing the mitochondrial import signal. We demonstrate that the NMR spectrum of...	nmrlearner	Journal club	0	04-10-2015 09:46 AM
[NMR paper] Selective observation of the disordered import signal of a globular protein by in-cell NMR: The example of frataxins. Selective observation of the disordered import signal of a globular protein by in-cell NMR: The example of frataxins. Selective observation of the disordered import signal of a globular protein by in-cell NMR: The example of frataxins. Protein Sci. 2015 Mar 12; Authors: Popovic M, Sanfelice D, Pastore C, Prischi F, Temussi PA, Pastore A Abstract We have exploited the capability of in-cell NMR to selectively observe flexible regions within folded proteins to carry out a comparative study of two members of the highly...	nmrlearner	Journal club	0	03-17-2015 05:12 PM
Selective observation of the disordered import signal of a globular protein by in-cell NMR: The example of frataxins Selective observation of the disordered import signal of a globular protein by in-cell NMR: The example of frataxins Abstract We have exploited the capability of in-cell NMR to selectively observe flexible regions within folded proteins to carry out a comparative study of two members of the highly conserved frataxin family which are found both in prokaryotes and in eukaryotes. They all contain a globular domain which shares more than 50% identity, which in eukaryotes is preceded by an N-terminal tail containing the mitochondrial import signal. We demonstrate that the NMR spectrum of the...	nmrlearner	Journal club	0	03-12-2015 11:38 PM
The BMRB matters The BMRB matters Nature Structural & Molecular Biology 19, 853 (2012) doi:10.1038/nsmb.2387 Published online 06 September 2012 NATURE STRUCTURAL & MOLECULAR BIOLOGY \| EDITORIAL http://www.nature.com/nsmb/journal/v19/n9/full/nsmb.2387.html	markber	General	0	11-27-2012 11:26 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