Unknown

Dataset Information

0

Hydrogen atoms in proteins: positions and dynamics.


ABSTRACT: Hydrogen atoms constitute about half of the atoms in proteins. Thus they contribute to the complex energy landscape of proteins [Frauenfelder, H., Sligar, S. G. & Wolynes, P. G. (1991) Science 254, 1598-1603]. Neutron crystal structure analysis was used to study the positions and mean-square displacements of hydrogen in myoglobin. A test of the reliability of calculated hydrogen atom coordinates by a comparison with our experimental results has been carried out. The result shows that >70% of the coordinates for hydrogen atoms that have a degree of freedom is predicted worse than 0.2 A. It is shown that the mean-square displacements of the hydrogen atoms obtained from the Debye-Waller factor can be divided into three classes. A comparison with the dynamic mean-square displacements calculated from the elastic intensities obtained from incoherent neutron scattering [Doster, W., Cusack, S. & Petry, W. (1989) Nature 337, 754-756] shows that mainly the side-chain hydrogen atoms contribute to dynamic displacements on a time scale faster than 100 ps.

SUBMITTER: Engler N 

PROVIDER: S-EPMC193546 | biostudies-literature | 2003 Sep

REPOSITORIES: biostudies-literature

altmetric image

Publications

Hydrogen atoms in proteins: positions and dynamics.

Engler Niklas N   Ostermann Andreas A   Niimura Nobuo N   Parak Fritz G FG  

Proceedings of the National Academy of Sciences of the United States of America 20030822 18


Hydrogen atoms constitute about half of the atoms in proteins. Thus they contribute to the complex energy landscape of proteins [Frauenfelder, H., Sligar, S. G. & Wolynes, P. G. (1991) Science 254, 1598-1603]. Neutron crystal structure analysis was used to study the positions and mean-square displacements of hydrogen in myoglobin. A test of the reliability of calculated hydrogen atom coordinates by a comparison with our experimental results has been carried out. The result shows that >70% of the  ...[more]

Similar Datasets

| S-EPMC2569941 | biostudies-literature
| S-EPMC6302931 | biostudies-literature
| S-EPMC6994207 | biostudies-literature
| S-EPMC5603579 | biostudies-literature
| S-EPMC7177507 | biostudies-literature
| S-EPMC3225823 | biostudies-literature
| S-EPMC8279655 | biostudies-literature
| S-EPMC3562696 | biostudies-literature
| S-EPMC4928899 | biostudies-literature
| S-EPMC5643538 | biostudies-literature