ArticleComputational and structural biotechnology journal2026
Lubricin's Mucin Domain Has Strong Polyproline Type II Helical Character.
Article in Computational and structural biotechnology journal, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Lubricin is a glycoprotein that is crucial for maintaining joint health by preventing joint wear through reducing joint friction in the boundary mode. Lubricin was recently observed to hinder the formation of uric acid crystals in the joint and prevent a form of gouty arthritis. However, despite lubricin's great physiological importance, our current understanding of the molecular origins of lubricin's beneficial properties is limited by a lack of detailed structural information regarding its central mucin domain: Lubricin's large size (227.5 kDa) and numerous glycosylations pose a substantial obstacle to conventional experimental methods for solving protein structures. In this work, we use a combination of physics-based replica exchange molecular dynamics simulations and circular dichroism experiments to shed light on the structure of lubricin's central mucin domain. Using replica exchange molecular dynamics, we model [KEPAPTTP]
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