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 08-21-2010, 04:03 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,615
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 Probing the structure and interactions of crystallin proteins by NMR spectroscopy.

Probing the structure and interactions of crystallin proteins by NMR spectroscopy.

Related Articles Probing the structure and interactions of crystallin proteins by NMR spectroscopy.

Prog Retin Eye Res. 1999 Jul;18(4):431-62

Authors: Carver JA

The lens is composed primarily of proteins, the crystallins, at high concentration whose structure and interactions are responsible for lens transparency. As there is no protein turnover in the majority of the lens, crystallin proteins have to be very stable and long-lived proteins. There are three types of crystallin proteins: alpha, beta and gamma, and they all are composed of a variety of subunits. In addition, extensive post-translational modification is undergone by many of the subunits. Determining the structural features and the preferential interactions and associations undergone by the crystallin proteins in the lens is a large and complex experimental undertaking. Some progress has been made in this area by X-ray crystallographic determination of structures for representative examples of the beta- and gamma-crystallins [Slingsby, C., Norledge, B., Simpson, A., Bateman, O. A., Wright, G., Driessen H. P. C., Lindley, P. F., Moss, D. S. and Bax, B. (1997) X-ray diffraction and structure of crystallins. Prog. Ret. Eye Res. 16, 3-29]. In this article, a summary is given of nuclear magnetic resonance (NMR) methods to determine information about these aspects of crystallin proteins. It is shown that despite their relatively large size, all crystallins give rise to well-resolved NMR spectra which arise from flexible terminal extensions that extend from the domain core of the proteins. By examining NMR spectra of mixtures of different crystallin subunits, it is possible to determine the role of these extensions in crystallin-crystallin interactions. For example, the flexible C-terminal extensions in the two alpha-crystallin subunits are not involved in interacting with the other crystallins but are crucially important in the chaperone action of alpha-crystallin. In this action, alpha-crystallin stabilises other proteins under conditions of stress, e.g. heat. In the lens, this ability probably has important consequences in preventing the precipitation of crystallin proteins with age and thereby contributing to cataract formation. The C-terminal extensions in alpha-crystallin act as solubilising agents for the protein and the high-molecular-weight complex that forms upon chaperone action with a precipitating "substrate" protein. Similar behaviour is observed for a variety of small heat-shock proteins, to which alpha-crystallin is related. NMR studies are also consistent with a two-domain structure for alpha-crystallin. No crystal structure is available for crystallin. Using the NMR data, a model for the quaternary structure of alpha-crystallin is proposed which comprises an annular arrangement for the subunits with a large central cavity.

PMID: 10217479 [PubMed - indexed for MEDLINE]



Source: PubMed
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
[NMR paper] Probing the binding entropy of ligand-protein interactions by NMR.
Probing the binding entropy of ligand-protein interactions by NMR. Related Articles Probing the binding entropy of ligand-protein interactions by NMR. Chembiochem. 2005 Sep;6(9):1585-91 Authors: Homans SW
nmrlearner Journal club 0 12-01-2010 06:56 PM
[NMR paper] Probing the kinetic landscape of transient peptide-protein interactions by use of pep
Probing the kinetic landscape of transient peptide-protein interactions by use of peptide (15)n NMR relaxation dispersion spectroscopy: binding of an antithrombin peptide to human prothrombin. Related Articles Probing the kinetic landscape of transient peptide-protein interactions by use of peptide (15)n NMR relaxation dispersion spectroscopy: binding of an antithrombin peptide to human prothrombin. J Am Chem Soc. 2003 Oct 15;125(41):12432-42 Authors: Tolkatchev D, Xu P, Ni F Protein-ligand interactions may lead to the formation of multiple...
nmrlearner Journal club 0 11-24-2010 09:16 PM
[NMR paper] Probing residual interactions in unfolded protein states using NMR spin relaxation te
Probing residual interactions in unfolded protein states using NMR spin relaxation techniques: an application to delta131delta. Related Articles Probing residual interactions in unfolded protein states using NMR spin relaxation techniques: an application to delta131delta. J Am Chem Soc. 2003 Oct 1;125(39):11988-92 Authors: Choy WY, Kay LE Residual interactions in delta131delta, a large disordered fragment of staphylococcal nuclease, have been probed at two different pHs using backbone (15)N and side-chain methyl (2)H NMR spin relaxation...
nmrlearner Journal club 0 11-24-2010 09:16 PM
[NMR paper] Probing proteins in solution by (129)Xe NMR spectroscopy.
Probing proteins in solution by (129)Xe NMR spectroscopy. Related Articles Probing proteins in solution by (129)Xe NMR spectroscopy. J Magn Reson. 2001 Jun;150(2):167-74 Authors: Locci E, Dehouck Y, Casu M, Saba G, Lai A, Luhmer M, Reisse J, Bartik K The interaction of xenon with different proteins in aqueous solution is investigated by (129)Xe NMR spectroscopy. Chemical shifts are measured in horse metmyoglobin, hen egg white lysozyme, and horse cytochrome c solutions as a function of xenon concentration. In these systems, xenon is in fast...
nmrlearner Journal club 0 11-19-2010 08:32 PM
[NMR paper] Probing site-specific interactions in protein-DNA complexes using heteronuclear NMR s
Probing site-specific interactions in protein-DNA complexes using heteronuclear NMR spectroscopy and molecular modeling: binding of Cro repressor to OR3. Related Articles Probing site-specific interactions in protein-DNA complexes using heteronuclear NMR spectroscopy and molecular modeling: binding of Cro repressor to OR3. J Biomol Struct Dyn. 1998 Aug;16(1):13-20 Authors: Edwards CA, Tung CS, Silks LA, Gatewood JM, Fee JA, Mariappan SV In this paper, a general method is developed to study site-specific interactions in DNA-protein complexes...
nmrlearner Journal club 0 11-17-2010 11:15 PM
[NMR paper] NMR spectroscopy of alpha-crystallin. Insights into the structure, interactions and c
NMR spectroscopy of alpha-crystallin. Insights into the structure, interactions and chaperone action of small heat-shock proteins. Related Articles NMR spectroscopy of alpha-crystallin. Insights into the structure, interactions and chaperone action of small heat-shock proteins. Int J Biol Macromol. 1998 May-Jun;22(3-4):197-209 Authors: Carver JA, Lindner RA The subunit molecular mass of alpha-crystallin, like many small heat-shock proteins (sHsps), is around 20 kDa although the protein exists as a large aggregate of average mass around 800...
nmrlearner Journal club 0 11-17-2010 11:06 PM
[NMR paper] Probing carbohydrate-protein interactions by high-resolution NMR spectroscopy.
Probing carbohydrate-protein interactions by high-resolution NMR spectroscopy. Related Articles Probing carbohydrate-protein interactions by high-resolution NMR spectroscopy. Adv Exp Med Biol. 1998;435:29-38 Authors: Homans SW, Field RA, Milton MJ, Probert M, Richardson JM
nmrlearner Journal club 0 11-17-2010 11:06 PM
[NMR paper] 1H-NMR spectroscopy of beta B2-crystallin from bovine eye lens. Conformation of the N
1H-NMR spectroscopy of beta B2-crystallin from bovine eye lens. Conformation of the N- and C-terminal extensions. 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 1H-NMR spectroscopy of beta B2-crystallin from bovine eye lens. Conformation of the N- and C-terminal extensions. Eur J Biochem. 1993 Apr 1;213(1):313-20 Authors: Carver JA, Cooper PG, Truscott RJ 1H-NMR spectroscopic studies of a 46-kDa homodimer, beta B2-crystallin,...
nmrlearner Journal club 0 08-21-2010 11:53 PM


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 - 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 04:45 AM.


Map