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point decrease » point increase (Expand Search)
d decrease » _ decrease (Expand Search), _ decreased (Expand Search), _ decreases (Expand Search)
a decrease » _ decrease (Expand Search), _ decreased (Expand Search), _ decreases (Expand Search)
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19281
Heterogeneous Condensation on Simplified Viral Envelope Protein Structures
Published 2025“…Complex glycoprotein structures were modeled as cylindrical pillars to analyze condensation rates and active surface areas across a range of <i>p/d</i> ratios (1.0, 1.2, 1.3, 1.7, 2.0, and ∞) and contact angles (θ = 15°, 75°, and 105°, corresponding to <i>f</i> = 3.0, 2.0, and 1.5) to address envelope geometries for a wide variety of viruses. …”
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19282
Heterogeneous Condensation on Simplified Viral Envelope Protein Structures
Published 2025“…Complex glycoprotein structures were modeled as cylindrical pillars to analyze condensation rates and active surface areas across a range of <i>p/d</i> ratios (1.0, 1.2, 1.3, 1.7, 2.0, and ∞) and contact angles (θ = 15°, 75°, and 105°, corresponding to <i>f</i> = 3.0, 2.0, and 1.5) to address envelope geometries for a wide variety of viruses. …”
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19283
Heterogeneous Condensation on Simplified Viral Envelope Protein Structures
Published 2025“…Complex glycoprotein structures were modeled as cylindrical pillars to analyze condensation rates and active surface areas across a range of <i>p/d</i> ratios (1.0, 1.2, 1.3, 1.7, 2.0, and ∞) and contact angles (θ = 15°, 75°, and 105°, corresponding to <i>f</i> = 3.0, 2.0, and 1.5) to address envelope geometries for a wide variety of viruses. …”
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19284
Heterogeneous Condensation on Simplified Viral Envelope Protein Structures
Published 2025“…Complex glycoprotein structures were modeled as cylindrical pillars to analyze condensation rates and active surface areas across a range of <i>p/d</i> ratios (1.0, 1.2, 1.3, 1.7, 2.0, and ∞) and contact angles (θ = 15°, 75°, and 105°, corresponding to <i>f</i> = 3.0, 2.0, and 1.5) to address envelope geometries for a wide variety of viruses. …”
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19285
Heterogeneous Condensation on Simplified Viral Envelope Protein Structures
Published 2025“…Complex glycoprotein structures were modeled as cylindrical pillars to analyze condensation rates and active surface areas across a range of <i>p/d</i> ratios (1.0, 1.2, 1.3, 1.7, 2.0, and ∞) and contact angles (θ = 15°, 75°, and 105°, corresponding to <i>f</i> = 3.0, 2.0, and 1.5) to address envelope geometries for a wide variety of viruses. …”
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19286
Heterogeneous Condensation on Simplified Viral Envelope Protein Structures
Published 2025“…Complex glycoprotein structures were modeled as cylindrical pillars to analyze condensation rates and active surface areas across a range of <i>p/d</i> ratios (1.0, 1.2, 1.3, 1.7, 2.0, and ∞) and contact angles (θ = 15°, 75°, and 105°, corresponding to <i>f</i> = 3.0, 2.0, and 1.5) to address envelope geometries for a wide variety of viruses. …”
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19287
Heterogeneous Condensation on Simplified Viral Envelope Protein Structures
Published 2025“…Complex glycoprotein structures were modeled as cylindrical pillars to analyze condensation rates and active surface areas across a range of <i>p/d</i> ratios (1.0, 1.2, 1.3, 1.7, 2.0, and ∞) and contact angles (θ = 15°, 75°, and 105°, corresponding to <i>f</i> = 3.0, 2.0, and 1.5) to address envelope geometries for a wide variety of viruses. …”
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19288
Heterogeneous Condensation on Simplified Viral Envelope Protein Structures
Published 2025“…Complex glycoprotein structures were modeled as cylindrical pillars to analyze condensation rates and active surface areas across a range of <i>p/d</i> ratios (1.0, 1.2, 1.3, 1.7, 2.0, and ∞) and contact angles (θ = 15°, 75°, and 105°, corresponding to <i>f</i> = 3.0, 2.0, and 1.5) to address envelope geometries for a wide variety of viruses. …”
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19289
Heterogeneous Condensation on Simplified Viral Envelope Protein Structures
Published 2025“…Complex glycoprotein structures were modeled as cylindrical pillars to analyze condensation rates and active surface areas across a range of <i>p/d</i> ratios (1.0, 1.2, 1.3, 1.7, 2.0, and ∞) and contact angles (θ = 15°, 75°, and 105°, corresponding to <i>f</i> = 3.0, 2.0, and 1.5) to address envelope geometries for a wide variety of viruses. …”
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19290
Heterogeneous Condensation on Simplified Viral Envelope Protein Structures
Published 2025“…Complex glycoprotein structures were modeled as cylindrical pillars to analyze condensation rates and active surface areas across a range of <i>p/d</i> ratios (1.0, 1.2, 1.3, 1.7, 2.0, and ∞) and contact angles (θ = 15°, 75°, and 105°, corresponding to <i>f</i> = 3.0, 2.0, and 1.5) to address envelope geometries for a wide variety of viruses. …”
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19291
Heterogeneous Condensation on Simplified Viral Envelope Protein Structures
Published 2025“…Complex glycoprotein structures were modeled as cylindrical pillars to analyze condensation rates and active surface areas across a range of <i>p/d</i> ratios (1.0, 1.2, 1.3, 1.7, 2.0, and ∞) and contact angles (θ = 15°, 75°, and 105°, corresponding to <i>f</i> = 3.0, 2.0, and 1.5) to address envelope geometries for a wide variety of viruses. …”
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19292
Heterogeneous Condensation on Simplified Viral Envelope Protein Structures
Published 2025“…Complex glycoprotein structures were modeled as cylindrical pillars to analyze condensation rates and active surface areas across a range of <i>p/d</i> ratios (1.0, 1.2, 1.3, 1.7, 2.0, and ∞) and contact angles (θ = 15°, 75°, and 105°, corresponding to <i>f</i> = 3.0, 2.0, and 1.5) to address envelope geometries for a wide variety of viruses. …”
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19293
Heterogeneous Condensation on Simplified Viral Envelope Protein Structures
Published 2025“…Complex glycoprotein structures were modeled as cylindrical pillars to analyze condensation rates and active surface areas across a range of <i>p/d</i> ratios (1.0, 1.2, 1.3, 1.7, 2.0, and ∞) and contact angles (θ = 15°, 75°, and 105°, corresponding to <i>f</i> = 3.0, 2.0, and 1.5) to address envelope geometries for a wide variety of viruses. …”
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19294
Heterogeneous Condensation on Simplified Viral Envelope Protein Structures
Published 2025“…Complex glycoprotein structures were modeled as cylindrical pillars to analyze condensation rates and active surface areas across a range of <i>p/d</i> ratios (1.0, 1.2, 1.3, 1.7, 2.0, and ∞) and contact angles (θ = 15°, 75°, and 105°, corresponding to <i>f</i> = 3.0, 2.0, and 1.5) to address envelope geometries for a wide variety of viruses. …”
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19295
Heterogeneous Condensation on Simplified Viral Envelope Protein Structures
Published 2025“…Complex glycoprotein structures were modeled as cylindrical pillars to analyze condensation rates and active surface areas across a range of <i>p/d</i> ratios (1.0, 1.2, 1.3, 1.7, 2.0, and ∞) and contact angles (θ = 15°, 75°, and 105°, corresponding to <i>f</i> = 3.0, 2.0, and 1.5) to address envelope geometries for a wide variety of viruses. …”
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19296
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19297
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19298
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19299
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19300