Temperature-dependent X-ray diffraction as a probe of protein structural dynamics

  title={Temperature-dependent X-ray diffraction as a probe of protein structural dynamics},
  author={Hans Frauenfelder and Gregory A. Petsko and Demetrius Tsernoglou},
X-ray diffraction at four temperatures from 220 to 300 K coupled with crystallographic refinement yields the mean-square displacements and conformational potentials of all 1,261 non-hydrogen atoms of metmyoglobin. The results are interpreted to indicate a condensed core around the haem, semi-liquid regions towards the outside and a possible pathway for ligands. It is concluded that X-ray diffraction can provide the spatial distribution of the dynamic features of a protein. 

Dynamics in alcohol dehydrogenase elucidated from crystallographic investigations.

  • S. Ramaswamy
  • Chemistry, Physics
    Advances in experimental medicine and biology
  • 1999
A major criticism of x-ray crystallographic studies of proteins is that they do not provide dynamic information. Crystallographic data provides time-averaged and space-averaged models. However,

X-Ray Diffuse Scattering from Protein Crystals

It is now well established that the biological activity of proteins is related not only to their mean molecular structure, but also to their intramolecular mobility (1). Nearly all techniques

Inter- and intramolecular motions in proteins

The use of 57 Fe Mossbauer radiation allows the study of protein crystal dynamics by a time-resolved analysis of X-ray scattering. In myoglobin crystals, the main source of the root mean squared

Structural Disorder in Myoglobin at Low Temperatures

This contribution discusses mainly low temperature aspects of protein dynamics. X-ray structure investigations of myoglobin between 300 K and 80 K give mean square displacements, , of the residues in

Distributions and Fluctuations of Protein Structures Investigated by X-Ray Analysis and Mössbauer Spectroscopy

The X-ray structure determination of myoglobin at five temperatures allows an estimation of the structural order at 0 K Extrapolation to 0 K of the x -values determined between 80 K and 300 K shows

Effects of temperature on protein structure and dynamics: X-ray crystallographic studies of the protein ribonuclease-A at nine different temperatures from 98 to 320 K.

Structures using X-ray diffraction data collected to 1.5-A resolution have been determined for the protein ribonuclease-A and it is determined that the protein molecule expands slightly with increasing temperature and that this expansion is linear.

Use of the neutron diffraction--H/D exchange technique to determine the conformational dynamics of trypsin.

A growing body of evidence indicates that conformational change is an important ingredient in a significant number of biological processes.

Evidence of Functional Protein Dynamics from X-Ray Crystallographic Ensembles

It is shown that measuring structural variations across an ensemble of X-ray derived models captures the activation of conformational states that are of functional importance just above TD, and that residue fluctuations measured in MD simulations at room temperature are in quantitative agreement with the experimental observable.



Crystallographic studies of the dynamic properties of lysozyme

It is concluded that protein mobility may play a significant part in biological activity and that X-ray crystallography can contribute to its analysis.

Dynamics of folded proteins

The dynamics of a folded globular protein have been studied by solving the equations of motion for the atoms with an empirical potential energy function and suggest that the protein interior is fluid-like in that the local atom motions have a diffusional character.

Picosecond dynamics of tyrosine side chains in proteins.

A dynamical analysis of the orientation fluctuations of two tyrosine side chains in the bovine pancreatic trypsin inhibitor is presented and it is found that the Langevin equation is applicable to the ring torsional motion, which corresponds to that of an angular harmonic oscillator with near-critical damping.

The Fluctuating Enzyme

The importance of random processes in generating conformational fluctuations in macromolecules which could be active towards catalysis is considered. The capability to correlate in time the

Subnanosecond motions of tryptophan residues in proteins.

  • I. MunroI. PechtL. Stryer
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 1979
The observed amplitudes and rates of these internal motions of tryptophan residues suggest that elementary steps in functionally significant conformational changes may take place in the subnanosecond time range.