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Dynamics of Molecular Hydrogen Exchange in Hydrogen-Bonded Systems

100%

Bureiko S. , Denisov G. S.

2002

tom Vol. 76 / nr 9

1177-1190

The kinetics of hydrogen exchange in molecular systems with H-bonds studied by kinetic IR spectroscopy and low-temperatureNMRspectroscopy methods is critically reviewed. The experimental rate constants and activation energies obtained so far for molecules capable of forming H-bonds as both proton donors and proton acceptors are collected and analyzed from the point of view of the influence of H-bond formation ability of the molecules- partners. The evidence available testifies to a molecular mechanism of the H-exchange reactions in inert solvents and in the gas phase via the formation of cyclic, mostly bimolecular, intermediates. The different mechanisms of the molecular H-exchange process in inert media are discussed and the possible paths of experimental elucidation of reaction mechanism are offered.

Methods of peptide conformation studies

100%

Bierzynski A.

Acta Biochimica Polonica

2001

tom 48

nr 4

In solution most of the peptides assume multiple flexible conformations. Determination of the dominant conformers and evaluation of their populations is the aim of pep- tide conformation studies, in which theoretical and experimental methods play complementary roles. Molecular dynamics or Monte Carlo methods are quite effective in searching the conformational space accessible to a peptide but they are not able to estimate, precisely enough, the populations of various conformations. Therefore, they must be supplemented by experimental data. In this paper, a short review of the experimental methods, most widely used in peptide conformational studies, is presented. Among them NMR plays the leading role. Valuable information is also obtained from hydrogen exchange, fluorescence resonance energy transfer, and circular dichroism measurements. The advantages and shortcomings of these methods are discussed.

Methods of peptide conformation studies.

88%

Biedrzyński A.

Acta Biochimica Polonica

2001

tom 48

nr 4

1091-1099

In solution most of the peptides assume multiple flexible conformations. Determination of the dominant conformers and evaluation of their populations is the aim of peptide conformation studies, in which theoretical and experimental methods play complementary roles. Molecular dynamics or Monte Carlo methods are quite effective in searching the conformational space accessible to a peptide but they are not able to estimate, precisely enough, the populations of various conformations. Therefore, they must be supplemented by experimental data. In this paper, a short review of the experimental methods, most widely used in peptide conformational studies, is presented. Among them NMR plays the leading role. Valuable information is also obtained from hydrogen exchange, fluorescence resonance energy transfer, and circular dichroism measurements. The advantages and shortcomings of these methods are discussed.