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



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 02-08-2011, 06:28 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 17,711
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 Solution NMR structure and dynamics of human apo-S100A1 protein.

Solution NMR structure and dynamics of human apo-S100A1 protein.

Solution NMR structure and dynamics of human apo-S100A1 protein.

J Struct Biol. 2011 Feb 2;

Authors: Nowakowski M, Jaremko L, Jaremko M, Zhukov I, Belczyk A, Bierzy?ski A, Ejchart A

S100A1 belongs to the EF-hand superfamily of calcium binding proteins. It is a representative of the S100 protein family based on amino acid sequence, three-dimensional structure, and biological function as a calcium signal transmitter. It is a homodimer of noncovalently bound subunits. S100A1, like most of other members of the S100 protein family, is a multifunctional, regulatory protein involved in a large variety of biological processes and closely associated with several human diseases. The three-dimensional structure of human apo-(i.e. calcium free)-S100A1 protein was determined by NMR spectroscopy (PDB 2L0P) and its backbone dynamics established by (15)N magnetic relaxation. Comparison of these results with the structure and backbone dynamics previously determined for bovine apo-S100A1 protein modified by disulfide formation with ?-mercaptoethanol at Cys85 revealed that the secondary structure of both these proteins was almost identical, whereas the global structure of the latter was much more mobile than that of human apo-S100 protein. Differences between the structures of human and rat apo-S100A1 are also discussed.

PMID: 21296671 [PubMed - as supplied by publisher]



Source: PubMed
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
Solution structure of the human Tax-interacting protein-1
Solution structure of the human Tax-interacting protein-1 Solution structure of the human Tax-interacting protein-1 Content Type Journal Article Pages 329-334 DOI 10.1007/s10858-009-9361-8 Authors
nmrlearner Journal club 0 01-09-2011 12:46 PM
[NMR paper] Solution NMR structure of the C-terminal domain of the human protein DEK.
Solution NMR structure of the C-terminal domain of the human protein DEK. Related Articles Solution NMR structure of the C-terminal domain of the human protein DEK. Protein Sci. 2004 Aug;13(8):2252-9 Authors: Devany M, Kotharu NP, Matsuo H The chromatin-associated protein DEK was first identified as a fusion protein in patients with a subtype of acute myelogenous leukemia. It has since become associated with diverse human ailments ranging from cancers to autoimmune diseases. Despite much research effort, the biochemical basis for these...
nmrlearner Journal club 0 11-24-2010 09:51 PM
[NMR paper] Three-dimensional solution structure of the calcium-signaling protein apo-S100A1 as d
Three-dimensional solution structure of the calcium-signaling protein apo-S100A1 as determined by NMR. Related Articles Three-dimensional solution structure of the calcium-signaling protein apo-S100A1 as determined by NMR. Biochemistry. 2002 Jan 22;41(3):788-96 Authors: Rustandi RR, Baldisseri DM, Inman KG, Nizner P, Hamilton SM, Landar A, Landar A, Zimmer DB, Weber DJ S100A1, a member of the S100 protein family, is an EF-hand containing Ca(2+)-binding protein (93 residues per subunit) with noncovalent interactions at its dimer interface. Each...
nmrlearner Journal club 0 11-24-2010 08:49 PM
[NMR paper] Characterization of the structure and dynamics of amyloidogenic variants of human lys
Characterization of the structure and dynamics of amyloidogenic variants of human lysozyme by NMR spectroscopy. Related Articles Characterization of the structure and dynamics of amyloidogenic variants of human lysozyme by NMR spectroscopy. Protein Sci. 2001 Dec;10(12):2525-30 Authors: Chamberlain AK, Receveur V, Spencer A, Redfield C, Dobson CM The structures and dynamics of the native states of two mutational variants of human lysozyme, I56T and D67H, both associated with non-neuropathic systemic amyloidosis, have been investigated by NMR...
nmrlearner Journal club 0 11-19-2010 08:44 PM
[NMR paper] NMR solution structure of type II human cellular retinoic acid binding protein: impli
NMR solution structure of type II human cellular retinoic acid binding protein: implications for ligand binding. Related Articles NMR solution structure of type II human cellular retinoic acid binding protein: implications for ligand binding. Biochemistry. 1998 Sep 15;37(37):12727-36 Authors: Wang L, Li Y, Abildgaard F, Markley JL, Yan H The structure of human apo-cellular retinoic acid binding protein II (apo-CRABPII) in solution at pH 7.3 has been determined by NMR spectroscopy. The sequential assignments of the 1H, 13C, and 15N resonances...
nmrlearner Journal club 0 11-17-2010 11:15 PM
[NMR paper] Solution NMR structure and backbone dynamics of the major cold-shock protein (CspA) f
Solution NMR structure and backbone dynamics of the major cold-shock protein (CspA) from Escherichia coli: evidence for conformational dynamics in the single-stranded RNA-binding site. Related Articles Solution NMR structure and backbone dynamics of the major cold-shock protein (CspA) from Escherichia coli: evidence for conformational dynamics in the single-stranded RNA-binding site. Biochemistry. 1998 Aug 4;37(31):10881-96 Authors: Feng W, Tejero R, Zimmerman DE, Inouye M, Montelione GT The major cold-shock protein (CspA) from Escherichia...
nmrlearner Journal club 0 11-17-2010 11:15 PM
[NMR paper] Structure and dynamics of the human granulocyte colony-stimulating factor determined
Structure and dynamics of the human granulocyte colony-stimulating factor determined by NMR spectroscopy. Loop mobility in a four-helix-bundle protein. Related Articles Structure and dynamics of the human granulocyte colony-stimulating factor determined by NMR spectroscopy. Loop mobility in a four-helix-bundle protein. Biochemistry. 1994 Jul 19;33(28):8453-63 Authors: Zink T, Ross A, Lüers K, Cieslar C, Rudolph R, Holak TA Recombinant 15N- and 13C-labeled human granulocyte colony-stimulating factor (rh-metG-CSF) has been studied by 2D and 3D...
nmrlearner Journal club 0 08-22-2010 03:29 AM
[NMR paper] Characterization of the three-dimensional solution structure of human profilin: 1H, 1
Characterization of the three-dimensional solution structure of human profilin: 1H, 13C, and 15N NMR assignments and global folding pattern. Related Articles Characterization of the three-dimensional solution structure of human profilin: 1H, 13C, and 15N NMR assignments and global folding pattern. Biochemistry. 1993 Dec 21;32(50):13818-29 Authors: Metzler WJ, Constantine KL, Friedrichs MS, Bell AJ, Ernst EG, Lavoie TB, Mueller L Human profilin is a 15-kDa protein that plays a major role in the signaling pathway leading to cytoskeletal...
nmrlearner Journal club 0 08-22-2010 03:01 AM


Thread Tools Search this Thread
Search this Thread:

Advanced Search
Display Modes Rate This Thread
Rate This 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



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



Powered by vBulletin® Version 3.7.3
Copyright ©2000 - 2017, 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 06:53 PM.


Map