Structural and Functional Investigation of the Ag+/Cu+ Binding Domains of the Periplasmic AdaptorProtein SilB from Cupriavidus metallidurans CH34

		BioNMR > Educational resources > Journal club
Structural and Functional Investigation of the Ag+/Cu+ Binding Domains of the Periplasmic AdaptorProtein SilB from Cupriavidus metallidurans CH34

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

05-15-2016, 05:00 AM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,174

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

Structural and Functional Investigation of the Ag+/Cu+ Binding Domains of the Periplasmic AdaptorProtein SilB from Cupriavidus metallidurans CH34

Structural and Functional Investigation of the Ag+/Cu+ Binding Domains of the Periplasmic AdaptorProtein SilB from Cupriavidus metallidurans CH34

Biochemistry
DOI: 10.1021/acs.biochem.6b00022

More...

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
The CopC Family: Structural and Bioinformatic Insightsinto a Diverse Group of Periplasmic Copper Binding Proteins The CopC Family: Structural and Bioinformatic Insightsinto a Diverse Group of Periplasmic Copper Binding Proteins http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00175/20160406/images/medium/bi-2016-001758_0008.gif Biochemistry DOI: 10.1021/acs.biochem.6b00175 http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/bichaw/~4/NhUil9uehKc More...	nmrlearner	Journal club	0	04-06-2016 10:29 PM
Preparation of a functional GABARAP-lipid conjugate in nanodiscs and its investigation by solution NMR spectroscopy. Preparation of a functional GABARAP-lipid conjugate in nanodiscs and its investigation by solution NMR spectroscopy. Preparation of a functional GABARAP-lipid conjugate in nanodiscs and its investigation by solution NMR spectroscopy. Chembiochem. 2010 Sep 24;11(14):1967-70 Authors: Ma P, Mohrlüder J, Schwarten M, Stoldt M, Singh SK, Hartmann R, Pacheco V, Willbold D	nmrlearner	Journal club	0	01-21-2011 01:22 AM
[NMR paper] Structural rearrangements of the two domains of Azotobacter vinelandii rhodanese upon Structural rearrangements of the two domains of Azotobacter vinelandii rhodanese upon sulfane sulfur release: essential molecular dynamics, 15N NMR relaxation and deuterium exchange on the uniformly labeled protein. Related Articles Structural rearrangements of the two domains of Azotobacter vinelandii rhodanese upon sulfane sulfur release: essential molecular dynamics, 15N NMR relaxation and deuterium exchange on the uniformly labeled protein. Int J Biol Macromol. 2003 Dec;33(4-5):193-201 Authors: Cicero DO, Melino S, Orsale M, Brancato G, Amadei A,...	nmrlearner	Journal club	0	11-24-2010 09:16 PM
[NMR paper] NMR analysis of cbEGF domains gives new insights into the structural consequences of NMR analysis of cbEGF domains gives new insights into the structural consequences of a P1148A substitution in fibrillin-1. Related Articles NMR analysis of cbEGF domains gives new insights into the structural consequences of a P1148A substitution in fibrillin-1. Protein Eng. 1998 Nov;11(11):957-9 Authors: Whiteman P, Downing AK, Handford PA Fibrillin-1 is a modular glycoprotein and a major component of the 10-12 nm microfibrils of the extracellular matrix. Mutations in the fibrillin-1 (FBN 1) gene result in the connective tissue disease the...	nmrlearner	Journal club	0	11-17-2010 11:15 PM
NMR Characterization of Copper-Binding Domains 4-6 of ATP7B, NMR Characterization of Copper-Binding Domains 4-6 of ATP7B, http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi1008535/aop/images/medium/bi-2010-008535_0002.gif Biochemistry DOI: 10.1021/bi1008535 http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/bichaw/~4/5w8PZPbbOyQ More...	nmrlearner	Journal club	0	09-11-2010 01:25 AM
NMR Characterization of Copper-binding Domains 4-6 of ATP7B. NMR Characterization of Copper-binding Domains 4-6 of ATP7B. Related Articles NMR Characterization of Copper-binding Domains 4-6 of ATP7B. Biochemistry. 2010 Aug 27; Authors: Fatemi N, Korzhnev DM, VÄ?lyvis A, Sarkar B, Forman-Kay JD The Wilson disease protein (ATP7B) is a copper-transporting member of the P-type ATPase superfamily, which plays a central role in copper homeostasis and interacts with the copper chaperone Atox1. The N-terminus of ATP7B is comprised of six copper-binding domains (WCBDs), each capable of binding one copper atom in the...	nmrlearner	Journal club	0	08-31-2010 09:42 PM
[NMR paper] An investigation of the ligand-binding site of the glutamine-binding protein of Esche An investigation of the ligand-binding site of the glutamine-binding protein of Escherichia coli using rotational-echo double-resonance NMR. Related Articles An investigation of the ligand-binding site of the glutamine-binding protein of Escherichia coli using rotational-echo double-resonance NMR. Biochemistry. 1994 Jul 26;33(29):8651-61 Authors: Hing AW, Tjandra N, Cottam PF, Schaefer J, Ho C Glutamine-binding protein (GlnBP) is an essential component of the glutamine transport system in Escherichia coli. Rotational-echo double-resonance...	nmrlearner	Journal club	0	08-22-2010 03:29 AM
[NMR paper] NMR investigation and secondary structure of domains I and II of rat brain calbindin NMR investigation and secondary structure of domains I and II of rat brain calbindin D28k (1-93). http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles NMR investigation and secondary structure of domains I and II of rat brain calbindin D28k (1-93). Eur J Biochem. 1999 Jun;262(3):933-8 Authors: Klaus W, Grzesiek S, Labhardt AM, Buchwald P, Hunziker W, Gross MD, Kallick DA Calbindin D28k, a member of the troponin C superfamily of...	nmrlearner	Journal club	0	08-21-2010 04:03 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