Carbon-13 nuclear magnetic resonance study of molecular motions and conformational transitions in muscle calcium binding parvalbumins

Abstract

The mirror carp (Cyprinus carpio) was studied. Nuclear relaxation parameters were used to evaluate the reorientation rates of the protein and some of the amino acid side chains. While peripheral residues exhibited greater motional freedom than the protein interior, an interesting finding was that significant rapid internal motion was present in the phenylalanine rings comprising the hydrophobic core of the protein.