X-Ray-Radiation-Induced Cooperative Atomic Movements in Protein

Petrova, T.; Lunin, Vladimir Y.; Ginell, Stephan L.; Hazemann, Isabelle; Lazarski, K.; Mitschler, A.; Podjarny, A.; Joachimiak, Andrzej

doi:10.1016/j.jmb.2009.02.030

Cited by 16 publications

(16 citation statements)

References 55 publications

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“…A comparison of the atomic coordinates for models corresponding to different stages of radiation damage revealed X-ray-induced displacements of the atoms of the elastase and water molecules. A similar phenomenon has recently been reported for aldose reductase (Petrova et al, 2009). Similar to the aldose molecule, the molecule of elastase expands with the increase in the absorbed dose.…”

Section: X-ray-induced Atomic Movementssupporting

confidence: 83%

“…In contrast, based on data on X-ray-induced changes in bond lengths in peptide crystals and radiolysis experiments, Meents and coworkers proposed that it is hydrogen abstraction from organic molecules with subsequent formation of gaseous hydrogen bubbles that causes global changes in the crystal (Meents et al, 2009(Meents et al, , 2010. Based on our recent experiments with aldose reductase, we suggested that the local damage is associated with global damage and that the linkage of these two processes is realised through the movement of protein domains and water molecules (Petrova et al, 2009). Our experiments showed that irradiation induced the movement of large parts of the protein globule, which occurred simultaneously with the decarboxylation of Asp and Glu residues involved in intermolecular contacts and the rearrangement of the water network.…”

Section: Introductionmentioning

confidence: 62%

“…Qualitatively, X-ray-induced structural changes were similar in all experiments. Local structural changes and domain movements in refined models were analyzed as described previously (Petrova et al, 2009).…”

Section: Resultsmentioning

confidence: 99%

“…Examples of X-ray-induced covalent-bond breakage are the disruption of disulfide bonds Weik et al, 2000;Burmeister, 2000); the rupture of covalent bonds between C and some heavy atoms, e.g. Se, Br, I and Hg (Evans et al, 2003;Ramagopal et al, 2005;Olié ric et al, 2007); the decarboxylation of glutamate and aspartate residues Burmeister, 2000;Fioravanti et al, 2007;Petrova et al, 2009) and the loss of the hydroxyl groups of tyrosines and the methylthio groups of methionines (Burmeister, 2000). It is believed that the atoms involved in ruptured bonds become mobile and diffuse through the sample.…”

Section: Introductionmentioning

confidence: 99%

“…Interestingly, these local changes do not affect all residues equally. For example, some glutamate and aspartate residues rapidly become decarboxylated in proportion to the X-ray dose; however, some remain intact and appear to be highly resistant to damage (Petrova et al, 2009).…”

Section: Introductionmentioning

confidence: 99%

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X-ray-induced deterioration of disulfide bridges at atomic resolution

Petrova¹,

Ginell²,

Mitschler³

et al. 2010

Acta Crystallogr D Biol Cryst

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Overall and site-specific X-ray-induced damage to porcine pancreatic elastase was studied at atomic resolution at temperatures of 100 and 15 K. The experiments confirmed that irradiation causes small movements of protein domains and bound water molecules in protein crystals. These structural changes occur not only at 100 K but also at temperatures as low as 15 K. An investigation of the deterioration of disulfide bridges demonstrated the following. (i) A decrease in the occupancy of S(γ) atoms and the appearance of new cysteine rotamers occur simultaneously. (ii) The occupancy decrease is observed for all S(γ) atoms, while new rotamers arise for some of the cysteine residues; the appearance of new conformations correlates with the accessibility to solvent. (iii) The sum of the occupancies of the initial and new conformations of a cysteine residue is approximately equal to the occupancy of the second cysteine residue in the bridge. (iv) The most pronounced changes occur at doses below 1.4 × 10(7) Gy, with only small changes occurring at higher doses. Comparison of the radiation-induced changes in an elastase crystal at 100 and 15 K suggested that the dose needed to induce a similar level of deterioration of the disulfide bonds and atomic displacements at 15 K to those seen at 100 K is more than two times higher.

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Section: X-ray-induced Atomic Movementssupporting

confidence: 83%

Section: Introductionmentioning

confidence: 62%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

X-ray-induced deterioration of disulfide bridges at atomic resolution

Petrova¹,

Ginell²,

Mitschler³

et al. 2010

Acta Crystallogr D Biol Cryst

Self Cite

View full text Add to dashboard Cite

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Direct Radiation Effects on the Structure and Stability of Collagen and Other Proteins

et al. 2019

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In this review, recent progress in understanding the direct effects of radiation on the structure and stability of collagen, the most abundant protein in the human body, and other proteins is surveyed. Special emphasis is placed on the triple‐helical structure of collagen, as studied by means of collagen mimetic peptides. The emerging patterns are the dose dependence of radiation processes and their abundance, the crucial role of radicals in covalent‐bond formation (crosslinking) or cleavage, and the influence of the radiation energy and nature. Future research should allow fundamental questions, such as charge transfer and fragmentation dynamics triggered by ionization, to be answered, as well as developing applications such as protein‐based biomaterials, notably with properties controlled by irradiation.

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