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

Go Back   BioNMR > Educational resources > NMR Questions and Answers
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 Rate Thread Display Modes
  #1  
Old 08-08-2008, 07:28 PM
Junior Member
 
Join Date: Aug 2008
Posts: 2
Points: 24, Level: 1
Points: 24, Level: 1 Points: 24, Level: 1 Points: 24, Level: 1
Level up: 47%, 26 Points needed
Level up: 47% Level up: 47% Level up: 47%
Activity: 0%
Activity: 0% Activity: 0% Activity: 0%
NMR Credits: 0
NMR Points: 24
Downloads: 0
Uploads: 0
Default Unanswered: peak intensity vs number of scans

Hi,
I have a question regarding how the peak intensities change when with increase in number of scans when the data is collected on a Varian NMR spectrometer. Suppose I collect a 15N-1H HSQC spectra with 8 scans and then collect the same spectra with 16 scans, would the peak intensities be double in the 16 scan spectra as compared to the 8 scan spectra? Does anyone know how the varian spectrometer scales the intensities according to the number of scans? Any suggestion or reply to my query will be extremely useful and greatly appreciated.

Thanks.
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
Peak height versus peak volume
Given a standard NOESY-based protein structure determination: Does anyone have any information on the benefits of measuring peak intensity by a volume integration method rather than simply measuring the peak height. Obviously integration is theoretically more accurate, but does it make any difference to the quality of the structures produced? especially if peak lineshapes are comparable? I was hoping to find some study comparing structures produced by both methods..... I'm also curious about the benefits of distance-calbrating NOEs to a curve rather than simply putting restraints...
paul NMR Questions and Answers 3 09-15-2015 07:48 PM
[NMR paper] Potential bias in NMR relaxation data introduced by peak intensity analysis and curve
Potential bias in NMR relaxation data introduced by peak intensity analysis and curve fitting methods. Related Articles Potential bias in NMR relaxation data introduced by peak intensity analysis and curve fitting methods. J Biomol NMR. 2001 Sep;21(1):1-9 Authors: Viles JH, Duggan BM, Zaborowski E, Schwarzinger S, Huntley JJ, Kroon GJ, Dyson HJ, Wright PE We present an evaluation of the accuracy and precision of relaxation rates calculated using a variety of methods, applied to data sets obtained for several very different protein systems. We...
nmrlearner Journal club 0 11-19-2010 08:44 PM
[NMRwiki tweet] nmrwiki: How is peak intensity related to J coupling in COSY? #nmrhttp://qa.nmrwiki.o
nmrwiki: How is peak intensity related to J coupling in COSY? #nmrhttp://qa.nmrwiki.org/question/197/ nmrwiki: How is peak intensity related to J coupling in COSY? #nmrhttp://qa.nmrwiki.org/question/197/ Source: NMRWiki tweets
nmrlearner Twitter NMR 0 11-18-2010 06:16 PM
[NMR paper] Automated peak picking and peak integration in macromolecular NMR spectra using AUTOP
Automated peak picking and peak integration in macromolecular NMR spectra using AUTOPSY. Related Articles Automated peak picking and peak integration in macromolecular NMR spectra using AUTOPSY. J Magn Reson. 1998 Dec;135(2):288-97 Authors: Koradi R, Billeter M, Engeli M, Güntert P, Wüthrich K A new approach for automated peak picking of multidimensional protein NMR spectra with strong overlap is introduced, which makes use of the program AUTOPSY (automated peak picking for NMR spectroscopy). The main elements of this program are a novel...
nmrlearner Journal club 0 11-17-2010 11:15 PM
[U. of Ottawa NMR Facility Blog] Dummy Scans
Dummy Scans Dummy scans (DS, Bruker) or steady state scans (SS, Varian) are scans taken in an NMR acquisition before the receiver is turned on and data are collected. Each dummy scan contains all of the rf pulses, delays and gradients used in the pulse program; the only difference is that the receiver is not turned on to collect data. Dummy scans are typically used to ensure that a spin system is in a steady state before data are collected. For example, One may collect a spectrum using a relaxation delay short with respect to the T1's of some of the resonances in the spectrum. The first...
nmrlearner News from NMR blogs 0 08-21-2010 08:15 PM
peak intensity vs number of scans
Hi, I have a question regarding how the peak intensities change when with increase in number of scans when the data is collected on a Varian NMR spectrometer. Suppose I collect a 15N-1H HSQC spectra with 8 scans and then collect the same spectra with 16 scans, would the peak intensities be double in the 16 scan spectra as compared to the 8 scan spectra? Does anyone know how the varian spectrometer scales the intensities according to the number of scans? Any suggestion or reply to my query will be extremely useful and greatly appreciated. Thanks.
aish1982 NMR software 0 08-08-2008 11:56 PM



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 PM.


Map