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, 03:01 AM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 17,582
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 15N NMR relaxation studies of the FK506 binding protein: backbone dynamics of the unc

15N NMR relaxation studies of the FK506 binding protein: backbone dynamics of the uncomplexed receptor.

Related Articles 15N NMR relaxation studies of the FK506 binding protein: backbone dynamics of the uncomplexed receptor.

Biochemistry. 1993 Sep 7;32(35):9000-10

Authors: Cheng JW, Lepre CA, Chambers SP, Fulghum JR, Thomson JA, Moore JM

Backbone dynamics of the major tacrolimus (FK506) binding protein (FKBP-12, 107 amino acids) have been studied using 15N relaxation data derived from proton-detected two-dimensional 1H-15N NMR spectroscopy. 15N spin-lattice relaxation rate constants (R1), spin-spin relaxation rate constants (R2), and heteronuclear NOEs were determined for over 85% of the backbone amide 15N nuclei. A model free formalism [Lipari, G., & Szabo, A. (1982) J. Am. Chem. Soc. 104, 4546-4559; Lipari, G., & Szabo, A. (1982) J. Am. Chem. Soc. 104, 4559-4570] was used to derive values for the generalized order parameter (S2), the effective correlation time for internal motions (tau e), and the chemical exchange line width (Rex) for each N-H bond vector. The final optimized overall correlation time (tau m) was 9.2 ns. The average order parameter (S2) describing the amplitude of motions on the picosecond time scale was found to be 0.88 +/- 0.06. Motions on the picosecond time scale are restricted at the N and C termini, consistent with previous NMR structural studies indicating well-defined beta-strands in these regions. With the exception of the flap region from resides 82 to 87, no regions appear to be significantly disordered on the picosecond time scale. Residues in several regions of the protein exhibit high Rex terms, indicating possible motions on the millisecond to microsecond time scale due to chemical exchange and/or conformational averaging effects. Possible effects of tacrolimus (FK506) binding on FKBP-12 dynamics are discussed in the context of previously determined solution structures for FKBP-12 in the uncomplexed [Michnick et al. (1991) Science 252, 836-839; Moore et al. (1991) Nature 351, 248-250] and complexed [Meadows et al. (1993) Biochemistry 32, 754-765] states.

PMID: 7690248 [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
Recent Developments in (15)N NMR Relaxation Studies that Probe Protein Backbone Dynamics.
Recent Developments in (15)N NMR Relaxation Studies that Probe Protein Backbone Dynamics. Recent Developments in (15)N NMR Relaxation Studies that Probe Protein Backbone Dynamics. Top Curr Chem. 2011 Sep 7; Authors: Ishima R Abstract Nuclear Magnetic Resonance (NMR) relaxation is a powerful technique that provides information about internal dynamics associated with configurational energetics in proteins, as well as site-specific information involved in conformational equilibria. In particular, (15)N relaxation is a useful probe to...
nmrlearner Journal club 0 09-08-2011 06:50 PM
[NMR paper] Backbone dynamics of the human MIA protein studied by (15)N NMR relaxation: implicati
Backbone dynamics of the human MIA protein studied by (15)N NMR relaxation: implications for extended interactions of SH3 domains. Related Articles Backbone dynamics of the human MIA protein studied by (15)N NMR relaxation: implications for extended interactions of SH3 domains. Protein Sci. 2003 Mar;12(3):510-9 Authors: Stoll R, Renner C, Buettner R, Voelter W, Bosserhoff AK, Holak TA The melanoma inhibitory activity (MIA) protein is a clinically valuable marker in patients with malignant melanoma as enhanced values diagnose metastatic...
nmrlearner Journal club 0 11-24-2010 09:01 PM
[NMR paper] Backbone dynamics of the c-Jun leucine zipper: 15N NMR relaxation studies.
Backbone dynamics of the c-Jun leucine zipper: 15N NMR relaxation studies. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Backbone dynamics of the c-Jun leucine zipper: 15N NMR relaxation studies. Biochemistry. 1996 Apr 16;35(15):4867-77 Authors: MacKay JP, Shaw GL, King GF The backbone dynamics of the coiled-coil leucine zipper domain of c-Jun have been studied using proton-detected two-dimensional 1H-15N NMR spectroscopy. Longitudinal (T1) and transverse (T2) 15N relaxation times,...
nmrlearner Journal club 0 08-22-2010 02:27 PM
[NMR paper] NMR studies of the FK506 binding protein bound to a spin-labeled ascomycin analog.
NMR studies of the FK506 binding protein bound to a spin-labeled ascomycin analog. Related Articles NMR studies of the FK506 binding protein bound to a spin-labeled ascomycin analog. J Magn Reson B. 1994 May;104(1):77-80 Authors: Yu L, Meadows RP, Wagner R, Fesik SW
nmrlearner Journal club 0 08-22-2010 03:33 AM
[NMR paper] 15N NMR relaxation studies of the FK506 binding protein: dynamic effects of ligand bi
15N NMR relaxation studies of the FK506 binding protein: dynamic effects of ligand binding and implications for calcineurin recognition. Related Articles 15N NMR relaxation studies of the FK506 binding protein: dynamic effects of ligand binding and implications for calcineurin recognition. Biochemistry. 1994 Apr 12;33(14):4093-100 Authors: Cheng JW, Lepre CA, Moore JM Backbone dynamics of the ligand- (FK506-) bound protein FKBP-12 (107 amino acids) have been examined using 15N relaxation data derived from inverse-detected two-dimensional...
nmrlearner Journal club 0 08-22-2010 03:33 AM
[NMR paper] NMR studies of the FK506 binding protein bound to a spin-labeled ascomycin analog.
NMR studies of the FK506 binding protein bound to a spin-labeled ascomycin analog. Related Articles NMR studies of the FK506 binding protein bound to a spin-labeled ascomycin analog. J Magn Reson B. 1994 May;104(1):77-80 Authors: Yu L, Meadows RP, Wagner R, Fesik SW
nmrlearner Journal club 0 08-22-2010 03:33 AM
[NMR paper] 15N NMR relaxation studies of the FK506 binding protein: dynamic effects of ligand bi
15N NMR relaxation studies of the FK506 binding protein: dynamic effects of ligand binding and implications for calcineurin recognition. Related Articles 15N NMR relaxation studies of the FK506 binding protein: dynamic effects of ligand binding and implications for calcineurin recognition. Biochemistry. 1994 Apr 12;33(14):4093-100 Authors: Cheng JW, Lepre CA, Moore JM Backbone dynamics of the ligand- (FK506-) bound protein FKBP-12 (107 amino acids) have been examined using 15N relaxation data derived from inverse-detected two-dimensional...
nmrlearner Journal club 0 08-22-2010 03:33 AM
[NMR paper] Heteronuclear 3D NMR studies of water bound to an FK506 binding protein/immunosuppres
Heteronuclear 3D NMR studies of water bound to an FK506 binding protein/immunosuppressant complex. Related Articles Heteronuclear 3D NMR studies of water bound to an FK506 binding protein/immunosuppressant complex. Biochemistry. 1993 Mar 16;32(10):2473-80 Authors: Xu RX, Meadows RP, Fesik SW From a series of 15N-resolved 3D ROESY-HMQC and 13C-resolved 3D NOESY-HMQC spectra of the FK506 binding protein (FKBP)/ascomycin complex in H2O, the locations of three tightly bound water molecules were identified. These waters are all buried within the...
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 - 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 11:21 AM.


Map