Rop protein: Difference between revisions

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== Mutants ==
== Mutants ==
Numerous mutations in the loop region of Rop have been produced (deletion of 5 a/a of loop ([[1b6q]]), site-directed mutants in loop, replacement and insertion of glycine residues in loop, restored of heptad pattern in loop region).
Numerous mutations in the loop region of Rop have been produced:
A31P appears to be trapped in a molten globule state, the reason being that Pro31, unlike Ala31, is more confor-mationally constrained (the dihedral angles of Ala31 in the wild type molecule are prohibited to Pro) and leads to a folding pathway for a thermodynamically less stable confor-mation.
*deletion of 5 a/a of loop [[(1qx8)]]
*site-directed mutants in loop  
*replacement and insertion of glycine residues in loop  
*restored of heptad pattern in loop region)[[(1NKD)]]
*a single alanine to proline substitution [[(1B6Q)]] (Pro31, unlike Ala31, is more confor-mationally constrained, the dihedral angles of Ala31 in the wild type molecule are prohibited to Pro, and leads to a folding pathway for a thermodynamically less stable conformation.)
*re-engineering topology of the homodimeric ROP protein into a single-chain 4-helix bundle[[(1YO7)]]
*ALA2ILE2-6, repacted the hydrophobic core and a new fold [[(1F4N)]]


*A31P [[1b6q]]
*RM6


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Student, Maria Amprazi, Nicole R Pendini, Keith Callenberg, David Canner, Jaime Prilusky, Michal Harel, Alexander Berchansky