ArticleJournal of molecular modeling2014
Structural and functional alterations of myoglobin by glucose-protein interactions.
Article in Journal of molecular modeling, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
7 citing papers in PubMed, 16 citations in OpenAlex.
- Glycogen Supplementation in Vitro Promotes pH Decline in Dark-Cutting Beef by Reverting Muscle's Metabolome toward a Normal Postmortem Muscle State.Journal of agricultural and food chemistry · 2024Article
- Identifying myoglobin as a mediator of diabetic kidney disease: a machine learning-based cross-sectional study.Scientific reports · 2022Article
- Pillar[RSC advances · 2022Review
- Effect of high intensity ultrasound on the structure and solubility of soy protein isolate-pectin complex.Ultrasonics sonochemistry · 2021Article
- Identification of the Protein Glycation Sites in Human Myoglobin as Rapidly Induced by d-Ribose.Molecules (Basel, Switzerland) · 2021Article
- Interactions Under Crowding Milieu: Chemical-Induced Denaturation of Myoglobin is Determined by the Extent of Heme Dissociation on Interaction with Crowders.Biomolecules · 2020Article
- Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The interaction of blood glucose with heme proteins plays a key role in inducing diabetes, a serious disease threatening human health. In this study, we investigated the non-covalent interaction between glucose and myoglobin (Mb), both theoretically and experimentally, using molecular dynamics (MD) simulation combined with spectroscopic studies. It revealed that glucoses can occupy the side pocket of Mb, and bind closely to one of the xenon cavities in Mb, by hydrogen bonding interactions with two propionate groups of heme as well as surrounding amino acids. These interactions alter the conformation of the heme active site slightly and lead to an enhanced peroxidase activity of Mb, as determined by kinetic studies. This study provides general information for glucose-heme proteins interactions, and also for blood glucose-protein interactions for patients with diabetes.
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Registered trials
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