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, 11:12 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 17,586
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 Conformational studies on a peptide fragment representing the RNA-binding N-terminus

Conformational studies on a peptide fragment representing the RNA-binding N-terminus of a viral coat protein using circular dichroism and NMR spectroscopy.

Related Articles Conformational studies on a peptide fragment representing the RNA-binding N-terminus of a viral coat protein using circular dichroism and NMR spectroscopy.

Eur J Biochem. 1991 Oct 15;201(2):489-94

Authors: van der Graaf M, Hemminga MA

Conformational studies were performed on a synthetic pentacosapeptide representing the RNA-binding N-terminal region of the coat protein of cowpea chlorotic mottle virus. The effects of ionic strength, addition of (oligo)phosphates and temperature on the conformation of this highly positively charged peptide containing six arginines and three lysines were studied. CD experiments show that the peptide has 15-18% alpha-helical conformation and about 80% random-coil conformation in the absence of inorganic salt at 25 degrees C, and 20-21% alpha-helical conformation under the same conditions at 10 degrees C. Addition of inorganic salts results in an increase of alpha-helix content, up to 42% in the presence of oligophosphate with an average chain length of 18 phosphates, which was used as an RNA analog. NMR experiments show that the alpha-helix formation starts in the region between Thr9 and Gln12, and is extended in the direction of the C terminus. Relaxation measurements show that binding to oligophosphates of increasing length results in reduced internal mobilities of the positively charged side chains of the arginyl and lysyl residues and of the side chain of Thr9 in the alpha-helical region. The alpha-helix formation in the N-terminal part of this viral coat protein upon binding of phosphate groups to the positively charged side chains is suggested to play an essential role in RNA binding.

PMID: 1935944 [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
Recombinant A22Gā??B31R-human insulin. A22 addition introduces conformational mobility in B chain C-terminus
Recombinant A22Gā??B31R-human insulin. A22 addition introduces conformational mobility in B chain C-terminus Recombinant A22Gā??B31R-human insulin. A22 addition introduces conformational mobility in B chain C-terminus Content Type Journal Article Category NMR structure note Pages 1-6 DOI 10.1007/s10858-012-9612-y Authors
nmrlearner Journal club 0 02-18-2012 10:58 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 paper] NMR studies of model peptides of PHGGGWGQ repeats within the N-terminus of prion prot
NMR studies of model peptides of PHGGGWGQ repeats within the N-terminus of prion proteins: a loop conformation with histidine and tryptophan in close proximity. Related Articles NMR studies of model peptides of PHGGGWGQ repeats within the N-terminus of prion proteins: a loop conformation with histidine and tryptophan in close proximity. J Biochem. 2000 Aug;128(2):271-81 Authors: Yoshida H, Matsushima N, Kumaki Y, Nakata M, Hikichi K The N-terminal region of the prion protein from human and mouse contains five tandem repeats with the consensus...
nmrlearner Journal club 0 11-19-2010 08:29 PM
[NMR paper] A conformational equilibrium in a protein fragment caused by two consecutive capping
A conformational equilibrium in a protein fragment caused by two consecutive capping boxes: 1H-, 13C-NMR, and mutational analysis. Related Articles A conformational equilibrium in a protein fragment caused by two consecutive capping boxes: 1H-, 13C-NMR, and mutational analysis. Protein Sci. 1998 Jul;7(7):1506-15 Authors: Guerois R, Cordier-Ochsenbein F, Baleux F, Huynh-Dinh T, Neumann JM, Sanson A The conformational properties of an 18 residues peptide spanning the entire sequence, L1KTPA5QFDAD10ELRAA15MKG, of the first helix (A-helix) of...
nmrlearner Journal club 0 11-17-2010 11:15 PM
[NMR paper] Structural analysis of peptide fragment 71-93 of transthyretin by NMR spectroscopy an
Structural analysis of peptide fragment 71-93 of transthyretin by NMR spectroscopy and electron microscopy: insight into amyloid fibril formation. Related Articles Structural analysis of peptide fragment 71-93 of transthyretin by NMR spectroscopy and electron microscopy: insight into amyloid fibril formation. Biochemistry. 1994 Jan 11;33(1):33-41 Authors: Jarvis JA, Munro SL, Craik DJ A peptide corresponding to the amino acid region 71-93 of the plasma protein transthyretin (TTR) has been synthesized to investigate its role in the native...
nmrlearner Journal club 0 08-22-2010 03:33 AM
[NMR paper] Structural analysis of peptide fragment 71-93 of transthyretin by NMR spectroscopy an
Structural analysis of peptide fragment 71-93 of transthyretin by NMR spectroscopy and electron microscopy: insight into amyloid fibril formation. Related Articles Structural analysis of peptide fragment 71-93 of transthyretin by NMR spectroscopy and electron microscopy: insight into amyloid fibril formation. Biochemistry. 1994 Jan 11;33(1):33-41 Authors: Jarvis JA, Munro SL, Craik DJ A peptide corresponding to the amino acid region 71-93 of the plasma protein transthyretin (TTR) has been synthesized to investigate its role in the native...
nmrlearner Journal club 0 08-22-2010 03:33 AM
[NMR paper] Solution conformation of a peptide fragment representing a proposed RNA-binding site
Solution conformation of a peptide fragment representing a proposed RNA-binding site of a viral coat protein studied by two-dimensional NMR. Related Articles Solution conformation of a peptide fragment representing a proposed RNA-binding site of a viral coat protein studied by two-dimensional NMR. Biochemistry. 1991 Jun 11;30(23):5722-7 Authors: van der Graaf M, van Mierlo CP, Hemminga MA The first 25 amino acids of the coat protein of cowpea chlorotic mottle virus are essential for binding the encapsidated RNA. Although an alpha-helical...
nmrlearner Journal club 0 08-21-2010 11:16 PM
[NMR paper] Conformational studies on a peptide fragment representing the RNA-binding N-terminus
Conformational studies on a peptide fragment representing the RNA-binding N-terminus of a viral coat protein using circular dichroism and NMR spectroscopy. 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 Conformational studies on a peptide fragment representing the RNA-binding N-terminus of a viral coat protein using circular dichroism and NMR spectroscopy. Eur J Biochem. 1991 Oct 15;201(2):489-94 Authors: van der Graaf M, Hemminga MA ...
nmrlearner Journal club 0 08-21-2010 11:12 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 04:05 PM.


Map