BioNMR
NMR aggregator & online community since 2003
BioNMR    
Learn or help to learn NMR - get free NMR books!
 

Go Back   BioNMR > Educational resources > Journal club
Advanced Search
Home Forums Wiki NMR feeds Downloads Register Today's Posts



Jobs Groups Conferences Literature Pulse sequences Software forums Programs Sample preps Web resources BioNMR issues


Webservers
NMR processing:
MDD
NMR assignment:
Backbone:
Autoassign
MARS
UNIO Match
PINE
Side-chains:
UNIO ATNOS-Ascan
NOEs:
UNIO ATNOS-Candid
UNIO Candid
ASDP
Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
XPLOR-NIH
ASDP
UNIO ATNOS-Candid
UNIO Candid
Fragment-based:
BMRB CS-Rosetta
Rosetta-NMR (Robetta)
Template-based:
GeNMR
I-TASSER
Refinement:
Amber
Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
BMRB CS-Rosetta
Homology-based:
CS23D
Simshift
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:
Shiftcor
UNIO Shiftinspector
LACS
CheckShift
RefDB
NMR model quality:
NOEs, other restraints:
PROSESS
PSVS
RPF scores
iCing
Chemical shifts:
PROSESS
CheShift2
Vasco
iCing
RDCs:
DC
Anisofit
Pseudocontact shifts:
Anisofit
Protein geomtery:
Resolution-by-Proxy
PROSESS
What-If
iCing
PSVS
MolProbity
SAVES2 or SAVES4
Vadar
Prosa
ProQ
MetaMQAPII
PSQS
Eval123D
STAN
Ramachandran Plot
Rampage
ERRAT
Verify_3D
Harmony
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:
camLILA
ccSOL
Camfold
camGroEL
Zyggregator
Isotope labeling:
UPLABEL
Solid-state NMR:
sedNMR


Reply
Thread Tools Search this Thread Rate Thread Display Modes
  #1  
Unread 08-17-2023, 09:13 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,192
Points: 193,617, Level: 100
Points: 193,617, Level: 100 Points: 193,617, Level: 100 Points: 193,617, Level: 100
Level up: 0%, 0 Points needed
Level up: 0% Level up: 0% Level up: 0%
Activity: 50.7%
Activity: 50.7% Activity: 50.7% Activity: 50.7%
Last Achievements
Award-Showcase
NMR Credits: 0
NMR Points: 193,617
Downloads: 0
Uploads: 0
Default Backbone and sidechain NMR assignments of residues 1-81 from yeast Sis1 in complex with an Hsp70 C-terminal EEVD peptide

Backbone and sidechain NMR assignments of residues 1-81 from yeast Sis1 in complex with an Hsp70 C-terminal EEVD peptide

Molecular chaperones aid proteins to fold and assemble without modifying their final structure, requiring, in several folding processes, the interplay between members of the Hsp70 and Hsp40 families. Here, we report the NMR chemical shift assignments for ¹ H, ^(15) N, and ^(13) C nuclei of the backbone and side chains of the J-domain of the class B Hsp40 from Saccharomyces cerevisiae, Sis1, complexed with the C-terminal EEVD motif of Hsp70. The data revealed information on the structure and...

More...
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
Class-specific interactions between Sis1 J-domain protein and Hsp70 chaperone potentiate disaggregation of misfolded proteins - pnas.org
Class-specific interactions between Sis1 J-domain protein and Hsp70 chaperone potentiate disaggregation of misfolded proteins - pnas.org Class-specific interactions between Sis1 J-domain protein and Hsp70 chaperone potentiate disaggregation of misfolded proteins pnas.org Read here
nmrlearner Online News 0 04-06-2022 11:19 AM
Class-specific interactions between Sis1 J-domain protein and Hsp70 chaperone potentiate disaggregation of misfolded proteins - pnas.org
Class-specific interactions between Sis1 J-domain protein and Hsp70 chaperone potentiate disaggregation of misfolded proteins - pnas.org Class-specific interactions between Sis1 J-domain protein and Hsp70 chaperone potentiate disaggregation of misfolded proteins pnas.org Read here
nmrlearner Online News 0 12-06-2021 11:12 PM
[NMR paper] Backbone and sidechain NMR assignments for the ribosome maturation factor RbfA from Escherichia coli.
Backbone and sidechain NMR assignments for the ribosome maturation factor RbfA from Escherichia coli. Related Articles Backbone and sidechain NMR assignments for the ribosome maturation factor RbfA from Escherichia coli. Biomol NMR Assign. 2020 Jul 15;: Authors: Schedlbauer A, Iturrioz I, Ochoa-Lizarralde B, Çapuni R, Han X, de Astigarraga E, Diercks T, Fucini P, Connell SR Abstract RbfA (ribosome binding factor A; 15.2*kDa) is a protein involved in ribosome biogenesis and has been shown to be important for growth at low...
nmrlearner Journal club 0 07-18-2020 10:53 AM
[NMR paper] Backbone and sidechain NMR assignments for the ribosome maturation factor RimP from Escherichia coli.
Backbone and sidechain NMR assignments for the ribosome maturation factor RimP from Escherichia coli. http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Backbone and sidechain NMR assignments for the ribosome maturation factor RimP from Escherichia coli. Biomol NMR Assign. 2020 Apr 17;: Authors: Schedlbauer A, Ochoa-Lizarralde B, Iturrioz I, Çapuni R, Diercks T, de Astigarraga E, Fucini P, Connell SR Abstract Ribosome biogenesis is...
nmrlearner Journal club 0 04-20-2020 05:10 PM
Easy and unambiguous sequential assignments of intrinsically disordered proteins by correlating the backbone 15 N or 13 Câ?² chemical shifts of multiple contiguous residues in highly resolved 3D spectra
Easy and unambiguous sequential assignments of intrinsically disordered proteins by correlating the backbone 15 N or 13 Câ?² chemical shifts of multiple contiguous residues in highly resolved 3D spectra Abstract Sequential resonance assignment strategies are typically based on matching one or two chemical shifts of adjacent residues. However, resonance overlap often leads to ambiguity in resonance assignments in particular for intrinsically disordered proteins. We investigated the potential of establishing connectivity through the three-bond couplings...
nmrlearner Journal club 0 01-12-2015 11:31 PM
[NMR paper] Backbone ¹H, ¹³C, ¹?N NMR assignments of yeast OMP synthase in unliganded form and in complex with orotidine 5'-monophosphate.
Backbone ¹H, ¹³C, ¹?N NMR assignments of yeast OMP synthase in unliganded form and in complex with orotidine 5'-monophosphate. http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Backbone ¹H, ¹³C, ¹?N NMR assignments of yeast OMP synthase in unliganded form and in complex with orotidine 5'-monophosphate. Biomol NMR Assign. 2014 Apr;8(1):103-8 Authors: Hansen MR, Harris R, Barr EW, Cheng H, Girvin ME, Grubmeyer C Abstract The...
nmrlearner Journal club 0 11-14-2014 08:33 AM
[NMR paper] Backbone and side-chain NMR assignments for the C-terminal domain of mammalian Vps28.
Backbone and side-chain NMR assignments for the C-terminal domain of mammalian Vps28. Related Articles Backbone and side-chain NMR assignments for the C-terminal domain of mammalian Vps28. Biomol NMR Assign. 2013 Dec 24; Authors: Peterson TA, Yu L, Piper RC Abstract Vps28 is one of four cytosolic proteins comprising the endosomal sorting complex required for transport I (ESCRT-I). ESCRT-I is involved in sorting ubiquitinated proteins to multivesicular bodies as well as in mediating budding of retroviruses. Here, we report the backbone...
nmrlearner Journal club 0 12-25-2013 03:39 PM
[NMR paper] Backbone 1H and 15N resonance assignments of the N-terminal SH3 domain of drk in fold
Backbone 1H and 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques. Related Articles Backbone 1H and 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques. J Biomol NMR. 1994 Nov;4(6):845-58 Authors: Zhang O, Kay LE, Olivier JP, Forman-Kay JD The backbone 1H and 15N resonances of the N-terminal SH3 domain of the Drosophila signaling adapter...
nmrlearner Journal club 0 08-22-2010 03:29 AM



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



BioNMR advertisements to pay for website hosting and domain registration. Nobody does it for us.



Powered by vBulletin® Version 3.7.3
Copyright ©2000 - 2024, Jelsoft Enterprises Ltd.
Copyright, BioNMR.com, 2003-2013
Search Engine Friendly URLs by vBSEO 3.6.0

All times are GMT. The time now is 11:06 AM.


Map