Regular Abstracts Submission Guidelines

  1. All participants are invited to submit more than one abstract.
  2. Abstracts MUST be submitted electronically via Online abstract submission form according to the following instructions by the deadline of September 15, 2010. Abstracts submitted by fax or by email will not be accepted.
  3. All abstracts will be peer reviewed. Each participant can select the form of the presentation Poster or Oral Presentation.
  4. Acceptance or rejection of an abstract is based on the average mark awarded by the reviewers.
  5. Presenting authors will be informed (by email) on the status of their abstract (accepted-rejected) by September 20, 2010.
  6. An abstract should contain maximum of 2500 characters/letters including spaces (approx. 250 words). The system will automatically let you know whether you complied with the rules before accepting your submission.
  7. Tables or/and pictures cannot be inserted.
  8. All abstracts must be written in English.
  9. Titles should not contain more than 20 words.
  10. No abbreviations are to be used in the titles.
  11. When submitting your abstract, consider the related Abstract Topics (see Abstract Topics).
  12. If you need to enter Greek letters or use bold, italics or superscript/subscript please use our special text editor by clicking on the 'edit' button.
  13. All accepted abstracts will be published in the Congress Handbook. Please note, that for each abstract accepted, the presenting author needs to be registered and the registration fee must be paid (before the deadline September 10, 2010 at the latest).
  14. Correction of abstracts can only be done before the deadline September 15, 2010.
  15. Abstracts received after the deadline cannot be considered for the Congress Handbook.

Required Abstract Structure and Formatting

Flexibility and plasticity of the structures of cytochromes P450 as a property determining their function

T. Smith1, E. Mc Donnald2

1 Palacky University, Pharmacology, Olomouc, Czech Republic
Charles University, Biochemistry, Prague, Czech Republic

Versatility of functions as well as of substrates of cytochromes P450 should be reflected in their ability to accommodate molecules of various size and shape. Active sites of cytochromes P450 hence differ in their flexibility and plasticity of the corresponding parts of the structure. Examples discussed here are cytochromes P450 known to metabolize various drugs and their analogs, namely, cytochromes P450 3A4, 2C9 and 2D6. Experimental data obtained by spectroscopic methods (absorption spectroscopy at high hydrostatic pressure and resonance Raman data) are correlated with results of molecular dynamic simulations carried out using the AMBER package with parm99 force field. Starting structures were essentially based on these taken from the PDB database; simulations were made at normal (0.1 MPa) and high pressure (300 MPa). The results indicate a decrease in radius of gyration as well as the overall B-factor decrease under high pressure. A correlation has been found between the experimentally obtained coefficient describing a shift of the Soret band with pressure (related to compressibility of the active site) and coordination numbers of water molecules and backbone atoms in the active site around the axial ligand (carbon monoxide). The data show that the spectral changes under pressure reflect structural changes in the close proximity (less than 0.5 nm) of the heme. The compressibility of the active site apparently increase with number of water molecules in the active site, and decrease with number of non-polar protein backbone atoms close to the heme. Raman spectral data reflect the situation in the active site by presence of heme vinyl vibrations assigned to two vinyl conformations, with two conformations present in the spectrum indicating a more flexible structure in the active site as e.g. in the case of CYP3A4. The data both experimental and obtained from the simulations hence document an essential necessity of plasticity/flexibility of enzyme active site for proper functioning of an enzyme, here cytochrome(s) P450.

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