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 11-17-2010, 11:06 PM
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 NMR structural studies on antifreeze proteins.

NMR structural studies on antifreeze proteins.

Related Articles NMR structural studies on antifreeze proteins.

Biochem Cell Biol. 1998;76(2-3):284-93

Authors: Sönnichsen FD, Davies PL, Sykes BD

Antifreeze proteins (AFPs) are a structurally diverse class of proteins that bind to ice and inhibit its growth in a noncolligative manner. This adsorption-inhibition mechanism operating at the ice surface results in a lowering of the (nonequilibrium) freezing point below the melting point. A lowering of approximately 1 degree C, which is sufficient to prevent fish from freezing in ice-laden seawater, requires millimolar AFP levels in the blood. The solubility of AFPs at these millimolar concentrations and the small size of the AFPs (typically 3-15 kDa) make them ideal subjects for NMR analysis. Although fish AFPs are naturally abundant, seasonal expression, restricted access to polar fishes, and difficulties in separating numerous similar isoforms have made protein expression the method of choice for producing AFPs for structural studies. Expression of recombinant AFPs has also facilitated NMR analysis by permitting isotopic labeling with 15N and 13C and has permitted mutations to be made to help with the interpretation of NMR data. NMR analysis has recently solved two AFP structures and provided valuable information about the disposition of ice-binding side chains in a third. The potential exists to solve other AFP structures, including the newly described insect AFPs, and to use solid-state NMR techniques to address fundamental questions about the nature of the interaction between AFPs and ice.

PMID: 9923697 [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
Crystallography reveals secrets of nature's antifreeze - physicsworld.com
<img alt="" height="1" width="1" /> Crystallography reveals secrets of nature's antifreeze physicsworld.com Ansgar Siemer of Columbia University in New York City, who has used nuclear magnetic resonance (NMR) to identify the ice-binding sites on antifreeze proteins, believes this detailed picture of the protein's structure will be useful to researchers. ... Crystallography reveals secrets of nature's antifreeze - physicsworld.com More...
nmrlearner Online News 0 04-13-2011 01:15 AM
Choosing membrane mimetics for NMR structural studies of transmembrane proteins.
Choosing membrane mimetics for NMR structural studies of transmembrane proteins. Choosing membrane mimetics for NMR structural studies of transmembrane proteins. Biochim Biophys Acta. 2011 Apr 5; Authors: Warschawski DE, Arnold AA, Beaugrand M, Gravel A, Chartrand E, Marcotte I The native environment of membrane proteins is complex and scientists have felt the need to simplify it to reduce the number of varying parameters. However, experimental problems can also arise from oversimplification which contributes to why membrane proteins are...
nmrlearner Journal club 0 04-12-2011 11:08 AM
Transferred NOESY NMR studies of biotin mimetic peptide (FSHPQNT) bound to streptavidin: A structural model for studies of peptide-protein interactions.
Transferred NOESY NMR studies of biotin mimetic peptide (FSHPQNT) bound to streptavidin: A structural model for studies of peptide-protein interactions. Transferred NOESY NMR studies of biotin mimetic peptide (FSHPQNT) bound to streptavidin: A structural model for studies of peptide-protein interactions. Chem Biol Drug Des. 2011 Feb 5; Authors: Gizachew D, Dratz E Protein-protein interactions control signaling, specific adhesion and many other biological functions. The three dimensional structures of the interfaces and bound ligand can be...
nmrlearner Journal club 0 02-08-2011 06:28 PM
NMR characterizations of the ice binding surface of an antifreeze protein.
NMR characterizations of the ice binding surface of an antifreeze protein. NMR characterizations of the ice binding surface of an antifreeze protein. PLoS One. 2010;5(12):e15682 Authors: Hong J, Hu Y, Li C, Jia Z, Xia B, Jin C Antifreeze protein (AFP) has a unique function of reducing solution freezing temperature to protect organisms from ice damage. However, its functional mechanism is not well understood. An intriguing question concerning AFP function is how the high selectivity for ice ligand is achieved in the presence of free water of...
nmrlearner Journal club 0 01-07-2011 11:21 PM
[NMR paper] Solid-state 17O NMR as a probe for structural studies of proteins in biomembranes.
Solid-state 17O NMR as a probe for structural studies of proteins in biomembranes. Related Articles Solid-state 17O NMR as a probe for structural studies of proteins in biomembranes. J Am Chem Soc. 2004 Dec 1;126(47):15320-1 Authors: Lemaître V, de Planque MR, Howes AP, Smith ME, Dupree R, Watts A We report the first example of 17O NMR spectra from a selectively labeled transmembrane peptide, 17O--WALP23, as a lyophilized powder and incorporated in hydrated phospholipid vesicles. It is shown that at high magnetic field it is feasible to apply...
nmrlearner Journal club 0 11-24-2010 10:03 PM
[NMR paper] Hydrogen bonding on the ice-binding face of a beta-helical antifreeze protein indicat
Hydrogen bonding on the ice-binding face of a beta-helical antifreeze protein indicated by amide proton NMR chemical shifts. Related Articles Hydrogen bonding on the ice-binding face of a beta-helical antifreeze protein indicated by amide proton NMR chemical shifts. Biochemistry. 2004 Oct 19;43(41):13012-7 Authors: Daley ME, Graether SP, Sykes BD The dependence of amide proton chemical shifts on temperature is used as an indication of the hydrogen bonding properties in a protein. The amide proton temperature coefficients of the beta-helical...
nmrlearner Journal club 0 11-24-2010 10:01 PM
[NMR paper] Characterization of threonine side chain dynamics in an antifreeze protein using natu
Characterization of threonine side chain dynamics in an antifreeze protein using natural abundance 13C NMR spectroscopy. Related Articles Characterization of threonine side chain dynamics in an antifreeze protein using natural abundance 13C NMR spectroscopy. J Biomol NMR. 2004 Jun;29(2):139-50 Authors: Daley ME, Sykes BD The dynamics of threonine side chains of the Tenebrio molitor antifreeze protein (TmAFP) were investigated using natural abundance (13)C NMR. In TmAFP, the array of threonine residues on one face of the protein is responsible...
nmrlearner Journal club 0 11-24-2010 09:51 PM
[NMR paper] An evaluation of detergents for NMR structural studies of membrane proteins.
An evaluation of detergents for NMR structural studies of membrane proteins. Related Articles An evaluation of detergents for NMR structural studies of membrane proteins. J Biomol NMR. 2004 Jan;28(1):43-57 Authors: Krueger-Koplin RD, Sorgen PL, Krueger-Koplin ST, Rivera-Torres IO, Cahill SM, Hicks DB, Grinius L, Krulwich TA, Girvin ME Structural information on membrane proteins lags far behind that on soluble proteins, in large part due to difficulties producing homogeneous, stable, structurally relevant samples in a membrane-like environment....
nmrlearner Journal club 0 11-24-2010 09:25 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 06:38 AM.


Map