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Retardation of the unfolding process by single N‐glycosylation of ribonuclease A based on molecular dynamics simulations

Biopolymers2007Vol. 89(2), pp. 114–123

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Young‐Jin Choi, Jong Hyun Lee, Suntae Hwang, J. E. Kim, Karpjoo Jeong, Seunho Jung

Abstract

The conformational characteristics of glycosylated- and unglycosylated bovine pancreatic ribonuclease A (RNaseA) were traced with unfolding molecular dynamics simulations using CHARMM program at 470 K. The glycosylated RNase (Glc_RNase) possesses nearly identical protein structure with RNaseA, differing only by presence of a single acetylglucosamine residue N-linked to Asn34 in the RNaseA. Attaching of monomeric N-acetylglucosamine residue to the Asn34 in RNaseA resulted in a change of denaturing process of Glc_RNase. Simulations showed that the unfolding of RNaseA involved significant weakening of nonlocal interactions whereas the glycosylation led Glc_RNase to preserve the nonlocal interactions even in its denatured form. Even in simulations over 8 ns at 470 K, Glc_RNase remained relatively stable as a less denatured conformation. However, conformation of RNaseA was changed to a fully unfolded state before 3 ns of the simulations at 470 K. This difference was due to fact that formation of hydrogen bond bridges and nonlocal contacts induced by the attached N-acetylglucosamine of Glc_RNase showing in the unfolding simulations. These high-temperature unfolding MD simulations provided a theoretical basis for the previous experimental work in which Glc_RNase showed slower unfolding kinetics compared with unglycosylated RNaseA, suggesting that single N-glycosylation induced retardation of unfolding process of the ribonuclease protein.

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Abstract

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