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 11-24-2010, 09:16 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,617
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 Structure of an elastin-mimetic polypeptide by solid-state NMR chemical shift analysi

Structure of an elastin-mimetic polypeptide by solid-state NMR chemical shift analysis.

Related Articles Structure of an elastin-mimetic polypeptide by solid-state NMR chemical shift analysis.

Biopolymers. 2003 Oct;70(2):158-68

Authors: Hong M, Isailovic D, McMillan RA, Conticello VP

The conformation of an elastin-mimetic recombinant protein, [(VPGVG)4(VPGKG)]39, is investigated using solid-state NMR spectroscopy. The protein is extensively labeled with 13C and 15N, and two-dimensional 13C-13C and 15N-13C correlation experiments were carried out to resolve and assign the isotropic chemical shifts of the various sites. The Pro 15N, 13Calpha, and 13Cbeta isotropic shifts, and the Gly-3 Calpha isotropic and anisotropic chemical shifts support the predominance of type-II beta-turn structure at the Pro-Gly pair but reject a type-I beta-turn. The Val-1 preceding Pro adopts mostly beta-sheet torsion angles, while the Val-4 chemical shifts are intermediate between those of helix and sheet. The protein exhibits a significant conformational distribution, shown by the broad line widths of the 15N and 13C spectra. The average chemical shifts of the solid protein are similar to the values in solution, suggesting that the low-hydration polypeptide maintains the same conformation as in solution. The ability to measure these conformational restraints by solid-state NMR opens the possibility of determining the detailed structure of this class of fibrous proteins through torsion angles and distances.

PMID: 14517905 [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
Solid-State NMR characterization of autofluorescent fibrils formed by the elastin-derived peptide GVGVAGVG.
Solid-State NMR characterization of autofluorescent fibrils formed by the elastin-derived peptide GVGVAGVG. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Solid-State NMR characterization of autofluorescent fibrils formed by the elastin-derived peptide GVGVAGVG. Biomacromolecules. 2011 May 9;12(5):1546-55 Authors: Sharpe S, Simonetti K, Yau J, Walsh P Abstract The characterization of the molecular structure and physical properties of self-assembling peptides is an...
nmrlearner Journal club 0 09-10-2011 06:51 PM
Solid-state NMR evidence for elastin-like beta-turn structure in spider dragline silk.
Solid-state NMR evidence for elastin-like beta-turn structure in spider dragline silk. Solid-state NMR evidence for elastin-like beta-turn structure in spider dragline silk. Chem Commun (Camb). 2010 Sep 28;46(36):6714-6 Authors: Jenkins JE, Creager MS, Butler EB, Lewis RV, Yarger JL, Holland GP Two-dimensional homo- and heteronuclear solid-state MAS NMR experiments on (13)C/(15)N-proline labeled Argiope aurantia dragline silk provide evidence for an elastin-like beta-turn structure for the repetitive Gly-Pro-Gly-X-X motif prevalent in major...
nmrlearner Journal club 0 12-28-2010 03:31 PM
[NMR paper] Magic-angle spinning solid-state NMR spectroscopy of the beta1 immunoglobulin binding domain of protein G (GB1): 15N and 13C chemical shift assignments and conformational analysis.
Magic-angle spinning solid-state NMR spectroscopy of the beta1 immunoglobulin binding domain of protein G (GB1): 15N and 13C chemical shift assignments and conformational analysis. Related Articles Magic-angle spinning solid-state NMR spectroscopy of the beta1 immunoglobulin binding domain of protein G (GB1): 15N and 13C chemical shift assignments and conformational analysis. J Am Chem Soc. 2005 Sep 7;127(35):12291-305 Authors: Franks WT, Zhou DH, Wylie BJ, Money BG, Graesser DT, Frericks HL, Sahota G, Rienstra CM Magic-angle spinning...
nmrlearner Journal club 0 12-01-2010 06:56 PM
[NMR paper] Structure distribution in an elastin-mimetic peptide (VPGVG)3 investigated by solid-s
Structure distribution in an elastin-mimetic peptide (VPGVG)3 investigated by solid-state NMR. Related Articles Structure distribution in an elastin-mimetic peptide (VPGVG)3 investigated by solid-state NMR. J Am Chem Soc. 2004 Apr 7;126(13):4199-210 Authors: Yao XL, Hong M Elastin is an extracellular-matrix protein that imparts elasticity to tissues. We have used solid-state NMR to determine a number of distances and torsion angles in an elastin-mimetic peptide, (VPGVG)3, to understand the structural basis of elasticity. C-H and C-N distances...
nmrlearner Journal club 0 11-24-2010 09:51 PM
[NMR paper] Investigation of the dynamics of an elastin-mimetic polypeptide using solid-state NMR
Investigation of the dynamics of an elastin-mimetic polypeptide using solid-state NMR. Related Articles Investigation of the dynamics of an elastin-mimetic polypeptide using solid-state NMR. Magn Reson Chem. 2004 Feb;42(2):267-75 Authors: Yao XL, Conticello VP, Hong M Elastin is the main structural protein that provides elasticity to various tissues and organs in vertebrates. Molecular motions are believed to play a significant role in its elasticity. We have used solid-state NMR spectroscopy to characterize the dynamics of an elastin-mimetic...
nmrlearner Journal club 0 11-24-2010 09:25 PM
[NMR paper] Measurement of conformational constraints in an elastin-mimetic protein by residue-pa
Measurement of conformational constraints in an elastin-mimetic protein by residue-pair selected solid-state NMR. Related Articles Measurement of conformational constraints in an elastin-mimetic protein by residue-pair selected solid-state NMR. J Biomol NMR. 2002 Feb;22(2):175-9 Authors: Hong M, McMillan RA, Conticello VP We introduce a solid-state NMR technique for selective detection of a residue pair in multiply labeled proteins to obtain site-specific structural constraints. The method exploits the frequency-offset dependence of cross...
nmrlearner Journal club 0 11-24-2010 08:49 PM
[NMR paper] Solid-state (13)C NMR reveals effects of temperature and hydration on elastin.
Solid-state (13)C NMR reveals effects of temperature and hydration on elastin. Related Articles Solid-state (13)C NMR reveals effects of temperature and hydration on elastin. Biophys J. 2002 Feb;82(2):1086-95 Authors: Perry A, Stypa MP, Tenn BK, Kumashiro KK Elastin is the principal protein component of the elastic fiber in vertebrate tissue. The waters of hydration in the elastic fiber are believed to play a critical role in the structure and function of this largely hydrophobic, amorphous protein. (13)C CPMAS NMR spectra are acquired for...
nmrlearner Journal club 0 11-24-2010 08:49 PM
Hi guys I need to help to restate this small pragraph? Chemical shift?solid state physics?
The chemical shift The chemical shift is one of the most important observables in nuclear magnetic resonance. It provides valuable information about the chemical environment around a nucleus. In a real spin system, nuclei are surrounded by atomic and molecular electron clouds which interact with the nuclear spin angular moment. The principal influence of the surrounding electrons is the magnetic screening which results when electronic orbitals are perturbed by the applied magnetic field BO. The effect of the magnetic screening (shielding), called nuclear shielding, can enhance or oppose the...
ISPolPH8789 NMR Questions and Answers 1 01-23-2005 03:06 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 08:16 AM.


Map