In <9303030148.AA12365 at net.bio.net> CZJ at CU.NIH.GOV writes:
> > While protonation is important in structure as well,
> > does anyone know of two structures of identical sequence
> > and pH/ligands having different structures?
>> The native state of a protein can best be described as a
> collection of conformations of similar free energy. If you
> pull up structures from the Protein DAta Bank that were
> determined by nmr, you will find that each file contains
> multiple structures. If you put these on your favorite
> graphics workstation, you will find several areas where the
> structures overlap almost completely. Other areas will show
> little agreement. There are areas of disorder, ie, multiple
Yes, there certainly are regions of multiple conformation in proteins.
However, it was my understanding that part of the reason that nmr
shows multiple conformations is that the surface of the protein is
less constrained by n.o.e. measurement so, de facto, protein surfaces
will show up as more mobile even if they are not.
Adrian Goldman | Internet: Goldman at Ala.BTK.UTu.Fi
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