Variation in Structure of a Protein (H2AX) with Knowledge-Based Interactions

Miriam Fritsche, Ras B Pandey, Barry L Farmer and Dieter W Heermann

PLOS ONE, 2013, vol. 8, issue 5, 1-6

Abstract: The structure of a protein (H2AX) as a function of temperature is examined by three knowledge-based phenomenological interactions, MJ (Miyazawa and Jernigan), BT (Betancourt and Thirumalai), and BFKV (Bastolla et al.) to identify similarities and differences in results. Data from the BT and BFKV residue-residue interactions verify finding with the MJ interaction, i.e., the radius of gyration (Rg) of H2AX depends non-monotonically on temperature. The increase in Rg is followed by a decay on raising the temperature with a maximum at a characteristic value, Tc, which depends on the knowledge-based contact matrix, TcBFKV ≤ TcMJ ≤ TcBT. The range (ΔT) of non-monotonic thermal response and its decay pattern with the temperature are sensitive to interaction. A rather narrow temperature range of ΔTMJ ≈ 0.015–0.022 with the MJ interaction expands and shifts up to ΔTBT ≈ 0.018–0.30 at higher temperatures with the BT interaction and shifts down with the BFKV interaction to ΔTBFKV ≈ 0.011–0.018. The scaling of the structure factor with the wave vector reveals that the structure of the protein undergoes a transformation from a random coil at high temperature to a globular conformation at low temperatures.

Date: 2013
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Citations: View citations in EconPapers (2)

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Persistent link: https://EconPapers.repec.org/RePEc:plo:pone00:0064507

DOI: 10.1371/journal.pone.0064507

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