1H NMR STRUCTURAL STUDIES OF A COMPLEX OF MELITTIN WITH PERDEUTERATED CALMODULIN
1987; Elsevier BV; Linguagem: Inglês
10.1016/b978-0-12-521040-9.50061-9
AutoresSteven H. Seeholzer, Mildred Cohn, A. Joshua Wand, Henry L. Crespi, John A. Putkey, Anthony R. Means,
Tópico(s)Bee Products Chemical Analysis
ResumoThis chapter explores several technical considerations for the successful application of 2-dimensional 1H-NMR methods to structural studies on the complexes of perdeuterated CaM (2H-CaM) with Mel and with the Mel (14–26) C-terminal half peptide (MLC). There are several technical problems associated with NMR studies of proteins and protein-protein complexes. The second class of 2D-NMR experiments rely on the incoherent transfer of magnetization between protons, which are near to one another in space. Because CaM is perdeuterated, the presence of two distinct spin systems for the indole ring protons of Mel's single Trp residue indicates that the ring exists in at least two conformations while bound to CaM. The effect of Mel, MLC, MLN and MLC plus MLN on the structure and dynamics of CaM were investigated in a series of ID NMR experiments. The specificity that Mel fragments show for binding to specific CaM domains may also be useful for illuminating some of the factors contributing to specificity in protein-protein interactions in general.
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