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Yazal, Jamal El

A5068007879 | I1330342723

Mayo Clinic

Mayo Clinic

Citations 7

Atomic levers control pyranose ring conformations

Proceedings of the National Academy of Sciences | July 26, 2002 | Volume: 96 | Issue: 14 | Pages: 7894-7898

10.1073/pnas.96.14.7894 | PMID 10393918

Atomic force microscope manipulations of single polysaccharide molecules have recently expanded conformational chemistry to include force-driven transitions between the chair and boat conformers of the pyranose ring structure. We now expand these observations to include chair inversion, a common phenomenon in the conformational chemistry of six-membered ring molecules. We demonstrate that by stretching single pectin molecules (1 → 4-linked α- d -galactouronic acid polymer), we could change the pyranose ring conformation from a chair to a boat and then to an inverted chair in a clearly resolved two-step conversion: 4 C 1 ⇄ boat ⇄ 1 C 4 . The two-step extension of the distance between the glycosidic oxygen atoms O 1 and O 4 determined by atomic force microscope manipulations is corroborated by ab initio calculations of the increase in length of the residue vector O 1 O 4 on chair inversion. We postulate that this conformational change results from the torque generated by the glycosidic bonds when a force is applied to the pectin molecule. Hence, the glycosidic bonds act as mechanical levers, driving the conformational transitions of the pyranose ring. When the glycosidic bonds are equatorial (e), the torque is zero, causing no conformational change. However, when the glycosidic bond is axial (a), torque is generated, causing a rotation around C—C bonds and a conformational change. This hypothesis readily predicts the number of transitions observed in pyranose monomers with 1a-4a linkages (two), 1a-4e (one), and 1e-4e (none). Our results demonstrate single-molecule mechanochemistry with the capability of resolving complex conformational transitions.
Zinc's Affect on Proton Transfer between Imidazole and Acetate Predicted by ab Initio Calculations

The Journal of Physical Chemistry B | July 26, 2002 | Volume: 104 | Issue: 28 | Pages: 6662-6667

10.1021/jp994283x

Proton Dissociation Energies of Zinc-Coordinated Hydroxamic Acids and Their Relative Affinities for Zinc:  Insight into Design of Inhibitors of Zinc-Containing Proteinases

The Journal of Physical Chemistry B | July 26, 2002 | Volume: 104 | Issue: 27 | Pages: 6499-6504

10.1021/jp0012707

Ab Initio Calculations of Proton Dissociation Energies of Zinc Ligands:  Hypothesis of Imidazolate as Zinc Ligand in Proteins

The Journal of Physical Chemistry B | July 26, 2002 | Volume: 103 | Issue: 41 | Pages: 8773-8779

10.1021/jp991787m

Novel Stable Configurations and Tautomers of the Neutral and Deprotonated Hydroxamic Acids Predicted from High-Level ab Initio Calculations

The Journal of Physical Chemistry A | July 26, 2002 | Volume: 103 | Issue: 41 | Pages: 8346-8350

10.1021/jp992203j

Heterodimeric Tacrine-Based Acetylcholinesterase Inhibitors:  Investigating Ligand−Peripheral Site Interactions

Journal of Medicinal Chemistry | July 26, 2002 | Volume: 42 | Issue: 20 | Pages: 4225-4231

10.1021/jm990224w | PMID 10514292

Protonation States of the Chromophore of Denatured Green Fluorescent Proteins Predicted by ab Initio Calculations

Journal of the American Chemical Society | July 26, 2002 | Volume: 122 | Issue: 46 | Pages: 11411-11415

10.1021/ja0008721