Stimuli, experiment procedure, and behavioral results.

Stimuli, experiment procedure, and behavioral results.

<p><b>(A)</b> Participants were seated back-to-back, facing separate but identical displays. Each participant had a keyboard to provide responses. <b>(B)</b> There were 16 unique grayscale stimuli, varying on 4 dimensions: spatial frequency (thick vs. thin lines), patte...

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Detaylı Bibliyografya
Yazar:	Denise Moerel (9080849) (author)
Diğer Yazarlar:	Tijl Grootswagers (9080843) (author), Genevieve L. Quek (12303518) (author), Sophie Smit (8129556) (author), Manuel Varlet (306580) (author)
Baskı/Yayın Bilgisi:	2025
Konular:	Neuroscience Evolutionary Biology Biological Sciences not elsewhere classified shared representations associated randomly matched pseudo interpret incoming information 45 &# 8211 200 &# 8201 180 &# 8201 neural processes underlying investigate information alignment alignment remain unknown cognitive processes early alignment upon rules successful cooperation stimulus presentation social interactions hyperscanning data extending beyond effectively captured categorization rules
Etiketler:	Etiketle Etiket eklenmemiş, İlk siz ekleyin!

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The time-course of information alignment, split by first and second experiment half.
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The contribution of shared rules to neural information alignment, for the first (A) and second (B) experiment half.
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Transfer task (pre- and post-test) design and information alignment.
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The time-course of information alignment.
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Information alignment between the two individuals in each pair.
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Individual memory performance was predicted by a subset of iEEG signal components.
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Patterns of connectivity were different depending on time alignment.
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Protein-lipid interactions in the <i>Surface</i> model.
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Energetics of protein interactions.
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Initial simulation coordinates.
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Snapshot showing cholesterol contacts with the N-terminus of p2 and H2 and H3 of p1 in the <i>Surface</i> model.
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Coulomb (electrostatic), Lennard-Jones (hydrophobic), and total interaction energy of interacting monomer helices in each model.
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Surface replica 4 structural evaluation.
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Tilt angle conformational landscapes of residues involved in 1-to-1 helix contacts during the last 500 ns of trajectory in the <i>Surface</i> model.
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Tilt angle conformational landscapes of residues involved in 1-to-1 helix contacts during the last 200 ns of trajectory in the <i>Sep</i> model.
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Contact maps of residues during the last half of trajectory (200 ns in <i>Sep</i> and 500 ns in <i>Surface</i> model), based on a cutoff of 14 Å.
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Distance of each amino acid from the average position of phosphorus atoms in the contacting membrane leaflet in the <i>Surface</i> systems.
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RMSF per residue in individual p7 monomers for each <i>Sep</i> and <i>Surface</i> model replicas.
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Root mean square deviation measurements of monomers.
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Deviations of the <i>Bound</i> model protein dimer conformation from the reference crystal structure of the channel (PDBID: 2M6X).
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Initial positioning of monomers in replicas 1, 2, 3 and 4 of <i>Surface</i> model.
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Baskı/Yayın Bilgisi: (2025)

List of protein residues and selected atoms to define the tilt angle vectors.
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Description of systems studied.
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