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Underlying structure in the dynamics of chase and escape interactions.

ABSTRACT: Chase and escape behaviors are important skills in many sports. Previous studies have described the behaviors of the attacker (escaper) and defender (chaser) by focusing on their positional relationship and have presented several key parameters that affect the outcome (successful attack or defense). However, it remains unclear how each individual agent moves, and how the outcome is determined in this type of interaction. To address these questions, we constructed a chase and escape task in a virtual space that allowed us to manipulate agents' kinematic parameters. We identified the basic strategies of each agent and their robustness to changes in their parameters. Moreover, we identified the determinants of the outcome and a geometrical explanation of their importance. Our results revealed the underlying structure of a simplified human chase and escape interaction and provided the insight that, although each agent apparently moves freely, their strategies in two-agent interactions are in fact rather constrained.

SUBMITTER: Tsutsui K

PROVIDER: S-EPMC6803680 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature

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Underlying structure in the dynamics of chase and escape interactions.

Tsutsui Kazushi K Shinya Masahiro M Kudo Kazutoshi K

Scientific reports 20191021 1

Chase and escape behaviors are important skills in many sports. Previous studies have described the behaviors of the attacker (escaper) and defender (chaser) by focusing on their positional relationship and have presented several key parameters that affect the outcome (successful attack or defense). However, it remains unclear how each individual agent moves, and how the outcome is determined in this type of interaction. To address these questions, we constructed a chase and escape task in a vir ...[more]

PMID: 31636328

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Project description:The human synuclein protein family includes alpha-synuclein, which has been linked to both familial and sporadic Parkinson's disease, and the highly homologous beta and gamma-synuclein. Mutations in alpha-synuclein cause autosomal dominant early onset Parkinson's, and the protein is found deposited in a fibrillar form in hereditary and idiopathic forms of the disease. No genetic link between beta and gamma-synuclein, and any neurodegenerative disease has been established, and it is generally considered that these proteins are not highly pathogenic. In addition, beta and gamma-synuclein are reported to aggregate less readily than alpha-synuclein in vitro. Indeed, beta-synuclein has been reported to protect against alpha-synuclein aggregation in vitro, as well as alpha-synuclein-mediated toxicity in vivo. Earlier, we compared the structural properties of the highly helical states adopted by all three synucleins in association with detergent micelles in an attempt to delineate the basis for functional differences between the three proteins. Here, we report a comparison of the structural and dynamic properties of the free states of all three proteins in order to shed light on differences that may help to explain their different propensities to aggregate, which in turn may underlie their differing contributions to the etiology of Parkinson's disease. We find that gamma-synuclein closely resembles alpha-synuclein in its free-state residual secondary structure, consistent with the more similar propensities of the two proteins to aggregate in vitro. beta-Synuclein, however, differs significantly from alpha-synuclein, exhibiting a lower predisposition towards helical structure in the second half of its lipid-binding domain, and a higher preference for extended structures in its C-terminal tail. Both beta and gamma-synuclein show less extensive transient long-range structure than that observed in alpha-synuclein. These results raise questions regarding the role of secondary structure propensities and transient long-range contacts in directing synuclein aggregation reactions.

Dataset Information

Underlying structure in the dynamics of chase and escape interactions.

Publications

Underlying structure in the dynamics of chase and escape interactions.

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