Following the structure analysis of uranocene, U(C{sub 8}H{sub 8}){sub 2}, we found to our surprise that almost nothing was known about the structure and bonding of organoactinides and lanthanides - ...a situation we have endeavored to change during the intervening years. The reported synthesis of uranocene in 1968 by Mueller-Westerhoff and Streitwieser sparked renewed interest in a field that had remained dormant since the synthesis of the cyclopentadienide compounds in the early 1950's. Two recent Accounts articles have described some of the subsequent developments in this field. A question which frequently occurs in discussions of this chemistry is: 'How covalent is the bonding in these compounds?' Within a careful and limited structural definition of covalent and ionic bonding, this question can be examined in some detail. This Account, while summarizing much of the structural information accumulated during the last ten years, will focus on the unifying structural trends in these compounds and the question of the mode of bonding. Complete reviews of the structural chemistry and further discussion of the structural aspects of the bonding can be found elsewhere. Our discussion will consider scandium and yttrium as lanthanides, based on their general chemical similarity to the true lanthanides.
The structures of five basic pancreatic trypsin inhibitor (BPTI) molecules are compared to establish the extent and nature of the conformational variability resulting from crystal packing effects. ...BPTI is an ideal system to evaluate such factors because of the availability of high resolution X-ray models of five different BPTI structures, each in a different crystal packing environment. Differences observed among the structures are found to be distributed throughout the molecule, although the regions that display most variability are associated with the loop structures (residues 14-17 and 24-29). The regions of structure that show the largest rms deviations from the mean of the five packing motifs correlate well with the presence of intermolecular contacts in the crystal lattice. For most of the molecules there is also a correspondence between a larger number of intermolecular contacts and systematically higher B-factors, although it is not apparent whether this is induced by the crystal contact or results from the fact that the contacts are made predominantly through surface loops. The conformational differences seen among the X-ray models constitute more than local shifts at the lattice contact surfaces, and in fact involve in some cases the making and breaking of intramolecular H-bonds. The magnitudes of the differences among packing models are significantly larger than those usually associated with changes induced by mutagenesis; for instance; the structural differences at the site of mutation observed on removing an internal disulfide from the molecule are significantly less than those associated with lattice contact effects. The crystal packing conformations are compared to representative structures of BPTI generated during a 96-psec molecular dynamics (MD) simulation. This comparison shows a high level of correspondence between the protein flexibility indicated by the X-ray and MD analyses, and specifically between those regions that are most variable. This suggests that the regions that show most variability among the crystal packing models are not artifacts of crystallization, but rather represent true low-energy conformers that have been preferentially selected by crystallization factors.
PDF
