Studies of calmodulin structure: laser raman spectroscopy of biomolecules. Academic Article uri icon

Overview

abstract

  • The structure of bovine brain calmodulin was probed by using laser Raman spectroscopy to elucidate cation-induced conformational changes in the protein. Local changes, most likely reflecting metal binding but not rearrangement of the peptide backbone, were observed in the presence of calcium or magnesium. A conformational change involving the peptide backbone and secondary structure content of calmodulin was observed only in the presence of calcium. The calcium-induced conformational change in the peptide backbone involves increased alpha helix and beta sheet. This was the only major calcium-specific change observed in the Raman spectrum, which suggests that the flexibility of the backbone conformation may play a critical role in the physiological activity of calmodulin.

publication date

  • February 15, 1983

Research

keywords

  • Calcium-Binding Proteins
  • Calmodulin

Identity

Scopus Document Identifier

  • 0021103357

Digital Object Identifier (DOI)

  • 10.1021/bi00273a041

PubMed ID

  • 6301532

Additional Document Info

volume

  • 22

issue

  • 4