BioNMR
NMR aggregator & online community since 2003
BioNMR    
Learn or help to learn NMR - get free NMR books!
 

Go Back   BioNMR > NMR community > News from NMR blogs
Advanced Search
Home Forums Wiki NMR feeds Downloads Register Today's Posts



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 Rating: Thread Rating: 1 votes, 5.00 average. Display Modes
  #1  
Old 05-10-2011, 07:07 AM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,777
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 Examples of Ramachandran plots of residues in helix, strand or coil regions

Examples of Ramachandran plots of residues in helix, strand or coil regions

Few weeks ago, I posted a blog that provides a newer collected/organized dataset for the torsional angles of proteins. I played around and try to use GnuPlot 4.4 to make my own Ramachandran plots. Here are three examples of the residual Ramachandran space regarding to the helical, extend or coil regions. I used STRIDE to [...]

Go to KPWU blog to read complete post.
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
Sequence correction of random coil chemical shifts: correlation between neighbor correction factors and changes in the Ramachandran distribution
Sequence correction of random coil chemical shifts: correlation between neighbor correction factors and changes in the Ramachandran distribution Abstract Random coil chemical shifts are necessary for secondary chemical shift analysis, which is the main NMR method for identification of secondary structure in proteins. One of the largest challenges in the determination of random coil chemical shifts is accounting for the effect of neighboring residues. The contributions from the neighboring residues are typically removed by using neighbor correction factors determined based on each...
nmrlearner Journal club 0 06-06-2011 12:53 AM
[NMR paper] Solid-state NMR data support a helix-loop-helix structural model for the N-terminal h
Solid-state NMR data support a helix-loop-helix structural model for the N-terminal half of HIV-1 Rev in fibrillar form. Related Articles Solid-state NMR data support a helix-loop-helix structural model for the N-terminal half of HIV-1 Rev in fibrillar form. J Mol Biol. 2001 Nov 2;313(4):845-59 Authors: Blanco FJ, Hess S, Pannell LK, Rizzo NW, Tycko R Rev is a 116 residue basic protein encoded by the genome of human immunodeficiency virus type 1 (HIV-1) that binds to multiple sites in the Rev response element (RRE) of viral mRNA transcripts in...
nmrlearner Journal club 0 11-19-2010 08:44 PM
[NMR paper] Prion protein fragments spanning helix 1 and both strands of beta sheet (residues 125
Prion protein fragments spanning helix 1 and both strands of beta sheet (residues 125-170) show evidence for predominantly helical propensity by CD and NMR. Related Articles Prion protein fragments spanning helix 1 and both strands of beta sheet (residues 125-170) show evidence for predominantly helical propensity by CD and NMR. Fold Des. 1998;3(5):313-20 Authors: Sharman GJ, Kenward N, Williams HE, Landon M, Mayer RJ, Searle MS BACKGROUND: Transmissible spongiform encephalopathies are a group of neurodegenerative disorders of man and animals...
nmrlearner Journal club 0 11-17-2010 11:06 PM
Complete (1)H, (13)C and (15)N NMR assignments for donor-strand complemented AafA, th
Complete (1)H, (13)C and (15)N NMR assignments for donor-strand complemented AafA, the major pilin of aggregative adherence fimbriae (AAF/II) from enteroaggregative E. coli. Related Articles Complete (1)H, (13)C and (15)N NMR assignments for donor-strand complemented AafA, the major pilin of aggregative adherence fimbriae (AAF/II) from enteroaggregative E. coli. Biomol NMR Assign. 2010 Aug 17; Authors: Yang Y, Berry AA, Lee WC, Garnett JA, Marchant J, Levine JA, Simpson PJ, Fogel SA, Varney KM, Matthews SJ, Nataro JP, Inman KG Aggregative...
nmrlearner Journal club 0 09-05-2010 05:53 AM
[NMR paper] The helix-hinge-helix structural motif in human apolipoprotein A-I determined by NMR
The helix-hinge-helix structural motif in human apolipoprotein A-I determined by NMR spectroscopy. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles The helix-hinge-helix structural motif in human apolipoprotein A-I determined by NMR spectroscopy. Biochemistry. 1997 Nov 4;36(44):13657-66 Authors: Wang G, Sparrow JT, Cushley RJ The conformation of a synthetic peptide of 46 residues from apoA-I was investigated by fluorescence, CD, and 2D NMR spectroscopies in lipid-mimetic environments....
nmrlearner Journal club 0 08-22-2010 05:08 PM
[NMR paper] High helicity of peptide fragments corresponding to beta-strand regions of beta-lacto
High helicity of peptide fragments corresponding to beta-strand regions of beta-lactoglobulin observed by 2D-NMR spectroscopy. Related Articles High helicity of peptide fragments corresponding to beta-strand regions of beta-lactoglobulin observed by 2D-NMR spectroscopy. Fold Des. 1996;1(4):255-63 Authors: Kuroda Y, Hamada D, Tanaka T, Goto Y BACKGROUND: Whereas protein fragments, when they are structured, adopt conformations similar to that found in the native state, the high helical propensity of beta-lactoglobulin, a predominantly beta-sheet...
nmrlearner Journal club 0 08-22-2010 02:27 PM
[NMR paper] PhoE signal peptide inserts into micelles as a dynamic helix-break-helix structure, w
PhoE signal peptide inserts into micelles as a dynamic helix-break-helix structure, which is modulated by the environment. A two-dimensional 1H NMR study. Related Articles PhoE signal peptide inserts into micelles as a dynamic helix-break-helix structure, which is modulated by the environment. A two-dimensional 1H NMR study. Biochemistry. 1995 Sep 12;34(36):11617-24 Authors: Chupin V, Killian JA, Breg J, de Jongh HH, Boelens R, Kaptein R, de Kruijff B Proteins that are destined for export out of the cytoplasm of Escherichia coli cells are...
nmrlearner Journal club 0 08-22-2010 03:50 AM
[NMR paper] Determination of helix-helix interactions in membranes by rotational resonance NMR.
Determination of helix-helix interactions in membranes by rotational resonance NMR. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Determination of helix-helix interactions in membranes by rotational resonance NMR. Proc Natl Acad Sci U S A. 1995 Jan 17;92(2):488-91 Authors: Smith SO, Bormann BJ Dimerization of human glycophorin A in erythrocyte membranes is mediated by specific interactions within the helical transmembrane domain of the protein. Rotational...
nmrlearner Journal club 0 08-22-2010 03:41 AM



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 Off
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 03:27 PM.


Map