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 08-22-2010, 03:29 AM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,135
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 Supramolecular order within the lens: 1H NMR spectroscopic evidence for specific crys

Supramolecular order within the lens: 1H NMR spectroscopic evidence for specific crystallin-crystallin interactions.

Related Articles Supramolecular order within the lens: 1H NMR spectroscopic evidence for specific crystallin-crystallin interactions.

Exp Eye Res. 1994 Nov;59(5):607-16

Authors: Cooper PG, Aquilina JA, Truscott RJ, Carver JA

alpha-, beta- and gamma-crystallins from bovine lens contain flexible terminal extensions which are readily observed by NMR spectroscopy. By monitoring these resonances, NMR spectroscopy therefore offers a means of examining specific protein-protein interactions in crystallin mixtures. In this paper, a 1H NMR spectroscopic study of bovine lens nuclear and cortical homogenates and various crystallin mixtures is presented. In both homogenates, resonances from the flexible C-terminal extensions of alpha-crystallin and the N-terminal extension of beta B2-crystallin are readily observed suggesting that these regions are not involved in crystallin-crystallin interactions. In the cortical homogenate, resonances from the short N-terminal extension of gamma S-crystallin are also present. The cortical homogenate gives rise to more intense resonances than the nuclear homogenate, suggesting that the cortical region has many more mobile crystallin regions. In both homogenates, the C-terminal extension of beta B2-crystallin and the very short C-terminal extension of gamma B-crystallin are not observed. Thus, the C-terminal regions of these proteins are involved in interactions with other crystallins. Similar effects are observed upon mixing of the individual crystallins, e.g. the C-terminal extension of gamma B-crystallin is absent in spectra of mixtures of total gamma-crystallin and high-molecular-weight beta-crystallin aggregates (beta H). Overall, the results are consistent with a short-range order for the crystallins within the lens.

PMID: 9492762 [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] Vitamin C metabolomic mapping in the lens with 6-deoxy-6-fluoro-ascorbic acid and hig
Vitamin C metabolomic mapping in the lens with 6-deoxy-6-fluoro-ascorbic acid and high-resolution 19F-NMR spectroscopy. Related Articles Vitamin C metabolomic mapping in the lens with 6-deoxy-6-fluoro-ascorbic acid and high-resolution 19F-NMR spectroscopy. Invest Ophthalmol Vis Sci. 2003 May;44(5):2047-58 Authors: Satake M, Dmochowska B, Nishikawa Y, Madaj J, Xue J, Guo Z, Reddy DV, Rinaldi PL, Monnier VM PURPOSE: Metabolomics, or metabolic profiling, is an emerging discipline geared to providing information on a large number of metabolites,...
nmrlearner Journal club 0 11-24-2010 09:01 PM
[NMR paper] TROSY and CRINEPT: NMR with large molecular and supramolecular structures in solution
TROSY and CRINEPT: NMR with large molecular and supramolecular structures in solution. Related Articles TROSY and CRINEPT: NMR with large molecular and supramolecular structures in solution. Trends Biochem Sci. 2000 Oct;25(10):462-8 Authors: Riek R, Pervushin K, Wüthrich K TROSY and CRINEPT are new techniques for solution NMR studies of molecular and supramolecular structures. They allow the collection of high-resolution spectra of structures with molecular weights >100 kDa, significantly extending the range of macromolecular systems that can...
nmrlearner Journal club 0 11-19-2010 08:29 PM
Supramolecular Interactions Probed by (13)C-(13)C Solid-State NMR Spectroscopy.
Supramolecular Interactions Probed by (13)C-(13)C Solid-State NMR Spectroscopy. Related Articles Supramolecular Interactions Probed by (13)C-(13)C Solid-State NMR Spectroscopy. J Am Chem Soc. 2010 Oct 8; Authors: Loquet A, Giller K, Becker S, Lange A We present a robust solid-state NMR approach for the accurate determination of molecular interfaces in insoluble and noncrystalline protein-protein complexes. The method relies on the measurement of intermolecular (13)C-(13)C distances in mixtures of glucose- and glucose-labeled proteins. We have...
nmrlearner Journal club 0 10-12-2010 02:52 PM
Supramolecular Interactions Probed by 13C-13C Solid-State NMR Spectroscopy
Supramolecular Interactions Probed by 13C-13C Solid-State NMR Spectroscopy Antoine Loquet, Karin Giller, Stefan Becker and Adam Lange http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja107460j/aop/images/medium/ja-2010-07460j_0003.gif Journal of the American Chemical Society DOI: 10.1021/ja107460j http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/jacsat/~4/uejHS045F6M
nmrlearner Journal club 0 10-09-2010 03:03 AM
[NMR paper] Comparative 1H-NMR studies on the physical state of water in soft contact lens and mo
Comparative 1H-NMR studies on the physical state of water in soft contact lens and mouse lens. Related Articles Comparative 1H-NMR studies on the physical state of water in soft contact lens and mouse lens. Biochim Biophys Acta. 1996 Apr 17;1289(3):369-76 Authors: Kuwata K, Era S, Sogami M, Amano H, Nagaoka S, Kato K, Takahashi K, Kitazawa Y, Watari H The physical state of water in mouse lenses (2-, 4- or 8-wk-old) and soft contact lenses (SCLs, water content from 18.4 to 79.2%) were studied by measuring spin-lattice relaxation times (T1) and...
nmrlearner Journal club 0 08-22-2010 02:27 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
Effect of site-specific variation of CSA and 15N chemical shielding tensor on model-free order parameter
:rolleyes: Variability of the 15N Chemical Shielding Tensors in the B3 Domain of Protein G from 15N Relaxation Measurements at Several Fields. Implications for Backbone Order Parameters Jennifer B. Hall and David Fushman J. Am. Chem. Soc., 128 (24), 7855 -7870, 2006.
nmrlearner Journal club 0 06-14-2006 11:17 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 - 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 12:33 AM.


Map