Different proteins do different things. Some adopt fewer conformations and a
more rigid structure after binding
a ligand, and others do the opposite. Haemoglobin is a nice example of a
protein that becomes a lot more flexible
after picking up ligands. For any reaction of the kind P + L -> PL ther
to complement the very nice description by jeremy, you may wish to try
and decompose the vibrational modes to get this sense by focussing on
the origins of the "red shift" in the vibrational spectrum and this
accounts largely for the increased vibrational entropies upon
complexation. This
Le Vendredi 7 Décembre 2012 18:48 CET, Gerard Bricogne
a écrit:
May I add something to Gerard's comment.
In the same vein, provided one does consider two sets of terms with zero mean
(which corresponds to the proviso mentioned by Gerard), one can define an
R-factor R as the sine of the same a
Good points have been brought up; here's one more to consider from my
experience. If you are going to run SEC prior to crystallization, I would
highly recommend running a native gel of the peak you collect. Especially
if you don't know the stoichiometry or if the stoichiometry is complex. I
crystal
Hi All
thanks for your detailed reply. A higher RMSF(as I showed in the png.) *doesnot
*mean that the RMSD for Calpha backbone showed be high. Am I correct ??
Because in my case the backbone RMSD for the receptor of the peptide bound
structure is lower than the receptor alone. Because I wanted to k
