3D Protein Structure Prediction with Local Adjust Tabu Search Algorithm

Lin, Xiao; Zhou, Fang

doi:10.1007/978-3-642-39678-6_18

Cited by 4 publications

(1 citation statement)

References 15 publications

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“…These proteins are highly underrepresented in proteomics study, as they are unsuitable for digestion in traditional aqueous medium, but are highly important in terms of drug targeting, diseases prediction, pharmacological, and biomedical studies. [2,23,24] Despite their promising potential as artificial proteases, soluble metal complexes such as POMs, are difficult to separate from the proteolytic mixture, which complicates further MS analysis. Therefore, the use of heterogeneous catalysis such as a metal organic frameworks (MOFs), could overcome this problem as the insoluble material can be removed from the reaction mixture via centrifugation.…”

Section: Introductionmentioning

confidence: 99%

Understanding the Role of Surfactants in the Interaction and Hydrolysis of Myoglobin by Zr‐MOF‐808

et al. 2022

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Controlled protein hydrolysis is an important procedure in proteomics applications and is used to aid the understanding of protein structure and function. The hydrolysis of hydrophobic proteins is particularly challenging, as due to their poor solubility the use of surfactants, which typically inactivate natural enzymes, is often required. Such limitations of natural enzymes prompted the development of chemical catalysts for the selective hydrolysis of proteins. In this study, the nanozymatic potential of MOF-808, a Zr 6 O 8 based metal organic framework, has been investigated towards protein hydrolysis in the presence of several surfactants which differ in structure and polarity. The influence of ionic SDS (sodium dodecyl sulfate), neutral TX-100 (Triton X-100) and zwitterionic Zw3-12 (ndodecyl-N,N-dimethyl-3-ammonio-1-propanesulfonate) and CHAPS (3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate) surfactants on the hydrolysis of horse heart myoglo-bin in the presence of MOF-808 has been examined. The hydrolysis of horse heart myoglobin by MOF-808 was followed using sodium dodecyl sulfate poly(acrylamide) gel electrophoresis (SDS-PAGE), which showed that nanozymatic activity of MOF-808 can be tuned by using appropriate surfactants. To understand the observed reactivity patterns, the interactions between surfactant, MOF and protein were further investigated using a range of spectroscopic methods, which included Dynamic Light Scattering (DLS), 1 H NMR, UV-Vis, Circular Dichroism and UV-Vis Spectroscopy. While the presence of SDS increased the number of observed peptide fragments due to protein unfolding and increased protein-MOF interaction, the use of zwitterionic and neutral surfactant reduced the hydrolytic efficiency, most likely by hindering the efficient protein-MOF interaction.

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Section: Introductionmentioning

confidence: 99%