Title : The structure of Fis mutant Pro61Ala illustrates that the kink within the long alpha-helix is not due to the presence of the proline residue.

Pub. Date : 1994 Nov 18

PMID : 7961857






2 Functional Relationships(s)
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1 The influence of proline on bending of the alpha-helix was investigated by replacement of the proline residue located in the middle of the long alpha-helix of the Fis protein with alanine, serine, or leucine. Proline long intergenic non-protein coding RNA 1554 Homo sapiens
2 One of the alpha-helices, the B-helix, is kinked in the wild-type Fis protein by 20 degrees which was previously assumed to be caused solely by the presence of proline 61 in the center of the helix. Proline long intergenic non-protein coding RNA 1554 Homo sapiens