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The crystal structure of the liganded form of a cytochrome c' shows significant structural changes that may be connected with dimer dissociation while NMR studies show how a single electron can cause a large repositioning of a cytochrome P450 substrate.
The first high resolution structures of the kinesin and NCD motor proteins reveal their surprising similarity to myosin but leave open the tantalizing question of what properties determine the directionality of movement along microtubules.
The solution structure of the peptide nucleic acid (PNA)-DNA hybrid GCTATGTC·d(GACATAGC) reveals a new duplex conformation and demonstrates that PNA can conform to nucleic acid partners of different conformations.
Paramagnetic relaxation measurements show that reduction of the cytochrome P450 BM3–substrate complex is accompanied by a structural change leading to a 6 Å movement of the substrate into the correct position and orientation for hydroxylation.
