[Characteristics of distribution of amino acid residues in the primary structure of calmodulin].
Systemic analysis of the peculiarities of distribution of di-, tri- and tetrapeptide residues in amino acid sequence of calmodulins of different origin has been carried out. A conclusion is made that all the examined repeated tri- and tetrapeptide residues with comparatively low conformation mobility enter the alpha-helical conformations with low mobility in beta-turns, and tri- and tetrapeptides with intermediate meaning of conformation entropy in beta-sheet conformations of the calmodulin molecule.
Pansevich
L I
LI
Barkovskiĭ
E V
EV
D000595:Amino Acid Sequence; D000818:Animals; D002147:Calmodulin / Q000737:chemistry*; D008969:Molecular Sequence Data; D011487:Protein Conformation; D051381:Rats; D013045:Species Specificity; D013816:Thermodynamics
D002147:Calmodulin
Osobennosti raspredeleniia sochetaniĭ aminokislotnykh ostatkov v pervichnoĭ strukture kal'modulina.