Yes, Bryan is right. This idea is totally 1970s, but with the smaller 
concentrators (microcons) and the smaller spec (nanodrop or equivalent.) 
Actually, since you have a lot of protein, you could scale it up more to avoid 
needing the nanodrop. But, most departments seem to have a nanodrop somewhere, 
as they are relatively cheap and pretty useful--perhaps ask around.

Jacob

  ----- Original Message ----- 
  From: Prince, D Bryan 
  To: [email protected] 
  Sent: Wednesday, August 04, 2010 9:33 AM
  Subject: Re: [ccp4bb] I-TASSER predicts NADPH binding, need to confirm with 
experiment



  Dear Xuan, 

   

  I am not certain, but I think that Jacob was referring to a spectrophotometer 
called a Nanodrop. It is available from ThermoFisher Scientific and can provide 
absorbance data on as little as 2uL of sample. I think that if you have access 
to a Nanodrop, and use Ultrafree 0.5mL concentrators, you can achieve the 
results that Jacob described. 

   

  Hope that helps, 

   

  Bryan

   





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  From: CCP4 bulletin board [mailto:[email protected]] On Behalf Of Xuan 
Yang
  Sent: Wednesday, August 04, 2010 9:46 AM
  To: [email protected]
  Subject: Re: [ccp4bb] I-TASSER predicts NADPH binding, need to confirm with 
experiment

   

  Dear Jacob,

   

  Nanodrop ultrafiltration sounds really fancy to me. I am afraid that I have 
no access to such equipment yet.

  Thanks for letting me know about this new technology.

   

  Sincerely,

   

  Xuan Yang

  2010/8/4 Jacob Keller <[email protected]>

  I like nanodrop ultrafiltration:

  concentrate your protein to the highest stable concentration possible

  figure out what is the lowest possible robustly-detectable nadph signal on 
your nanodrop

  combine the two in such a way in the top of a microcon of appropriate MWCO to 
acheive the highest possible protein concentration with the lowest possible 
nadph concentration. Take a baseline spec reading before spinning.

  spin long enough to get enough flowthrough to measure on the nano (~10uL is 
plenty.) Flowthrough should be the free nadph concentration L. Total L should 
be known, as well as total P, so you can figure out bound concentrations PL 
easily.

  you should probable do this in triplicate or so, with appropriate controls. I 
found 50uL/microcon to be a good balance of pipette-ability and economy of 
protein. If you want to get fancier, you can do more samples varying 
concentrations (or do some other more sophisticated method.)

  Jacob 






  On Wed, Aug 4, 2010 at 3:10 AM, Xuan Yang <[email protected]> wrote:

  Dear All,

   

  3D structure modeling server I-TASSER predicts a binding site for NADPH and I 
want to test this prediction. What would be the nice quick way to tell whether 
this protein bind NADPH or not, when I have a lot of recombinant protein? 

   

  Sincerely,

   

  Xuan Yang

   

   












*******************************************
Jacob Pearson Keller
Northwestern University
Medical Scientist Training Program
Dallos Laboratory
F. Searle 1-240
2240 Campus Drive
Evanston IL 60208
lab: 847.491.2438
cel: 773.608.9185
email: [email protected]
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