To: CCP4BB@JISCMAIL.AC.UK
Subject: Re: [ccp4bb] nmr question
There are about 20 structures solved by NMR with chain lengths above 300
residues. Some of them are solved by combination of restraints and modeling
(e.g. 2010 Nature paper describing implementation of Rosetta modeling coupled
with backbone
...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
'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
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
Dear members,
I know that it is not possible to solve a structure by nmr of more than
approx. 30 kda. But I have to admit that I dont know why. What exactly is
overlapping?
With best regards,
Lena
There are about 20 structures solved by NMR with chain lengths above 300
residues. Some of them are solved by combination of restraints and modeling
(e.g. 2010 Nature paper describing implementation of Rosetta modeling
coupled with backbone-only data, by Raman/Montelione/Baker et al.).
Principal
