Title : Cation binding and conformation of human calmodulin-like protein.

Pub. Date : 1993 Jun 15

PMID : 8507643






2 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Conformational changes in the unique Tyr138 microenvironment, monitored by fluorimetry and near-UV difference spectrophotometry, indicate that in metal-free CLP this Tyr is shielded from the polar solvent and strongly quenched by a specific chemical group; Ca2+ binding induces a shift of Tyr to a more polar environment and removal of the quenching group, but without full exposure to the solvent. Tyrosine calmodulin like 3 Homo sapiens
2 Conformational changes in the unique Tyr138 microenvironment, monitored by fluorimetry and near-UV difference spectrophotometry, indicate that in metal-free CLP this Tyr is shielded from the polar solvent and strongly quenched by a specific chemical group; Ca2+ binding induces a shift of Tyr to a more polar environment and removal of the quenching group, but without full exposure to the solvent. Tyrosine calmodulin like 3 Homo sapiens