NMR people do collect NMR data beyond 40 deg C. Many membrane protein structures are determined at 55-60 deg .C (the membrane proteins may not be very large but in micelles -combined weight is large). When the protein is stable and the 1H-15N-HSQC (fingerprint region) does not change with temp (meaning temp has no effect on the protein), one can go higher temp. Yes, it certainly helps reducing line width and if you combine TROSY based experiments, the resolution increases dramatically. Smita Mohanty
>>> Roopa Thapar <rtha...@hwi.buffalo.edu> 7/1/2011 11:47 AM >>> ‘NMR people’ do use thermophilic proteins but I have never heard of anyone boiling samples :) By increasing temperature I meant going to around 37-40 deg C. On 7/1/11 12:26 PM, "Jacob Keller" <j-kell...@fsm.northwestern.edu> wrote: >...they are stable enough that one can raise the temperature to increase the correlation time. I wonder whether NMR people have tried using hyperthermophile proteins to be able to essentially boil the sample to decrease the rotational correlation time constant? There is even an organism I read about in a Science brevia paper whose peak doubling time is at autoclave temperatures... JPK
