[fanning]

Hi, everyone

I am making some mutants of a Calcium channel, mainly interested in a Asp residue located in S4-S5 linker. When this Asp was mutated into Glu, the channel lost its function.

Given both Asp and Glu are negatively charged, and have similiar molecular weight, I wonder why this subtle change killed the channel. Does anybody know what is the major difference between these two amino acids, in terms of biochemistry properties, strutural biology or whatever?

Thank you very much.

Fanning

[AWK]

see asparitc and glutamic acid in COMMON NAMES (this forum)

[savoy7]

boy, that one carbon group must have made some structural difference in the protein

won't think it would - hmmm

Did you do a point mutation changing a pyrimidine w/a purine?
oops off task

I can't think of what that one carbon group would have done to the protein, except making that amino acid bigger which might change the structural shape of the channel.

sorry can't think of anything
savoy