Journal
JOURNAL OF PHYSICAL CHEMISTRY B
Volume 127, Issue 31, Pages 6887-6895Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.jpcb.3c02473
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Conformational dynamics in proteins can lead to aggregation-prone states during folding, resulting in the formation of oligomers and aggregates. This study investigated the intermediates and near-folded states of β2-microglobulin and their physico-chemical properties using molecular dynamics and Markov state modeling. Analysis of hundreds of microseconds of simulation revealed the importance of edge strands in misfolded states, which led to high exposure of hydrophobic residues in the protein core, initiating oligomerization and aggregate formation. This study sheds light on the initial steps of β2m monomer aggregation and provides a better understanding of protein misfolding and aggregation landscapes.
Conformationaldynamics in proteins can give rise to aggregationprone states during folding, and these kinetically stable states couldform oligomers and aggregates. In this study, we investigate the intermediatestates and near-folded states of & beta;2-microglobulin and theirphysico-chemical properties using molecular dynamics and Markov statemodeling. Analysis of hundreds of microseconds simulation show theimportance of the edge strands in the misfolded states that give riseto a high exposure of hydrophobic residues in the core of the proteinthat could initiate oligomerization and aggregate formation. Our studysheds light on the first step of aggregation of & beta;2m monomersand gave a better picture of the landscape of protein misfolding andaggregation.
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