Title : Interactions controlling the membrane binding of basic protein domains: phenylalanine and the attachment of the myristoylated alanine-rich C-kinase substrate protein to interfaces.

Pub. Date : 1999 Sep 28

PMID : 10504221






2 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 As expected, MARCKS-Ala binds more weakly to membranes composed of PS/PC (1:9) than does the native MARCKS peptide; however, each phenylalanine contributes only 0.2 kcal/mol to the binding energy difference, far less than the 1.3 kcal/mol expected for the binding of phenylalanine to the membrane interface. Phenylalanine myristoylated alanine rich protein kinase C substrate Homo sapiens
2 As expected, MARCKS-Ala binds more weakly to membranes composed of PS/PC (1:9) than does the native MARCKS peptide; however, each phenylalanine contributes only 0.2 kcal/mol to the binding energy difference, far less than the 1.3 kcal/mol expected for the binding of phenylalanine to the membrane interface. Phenylalanine myristoylated alanine rich protein kinase C substrate Homo sapiens