Oxyhemoglobin, R state
Human hemoglobin in the oxygen-bound R state. The classic structure that captures cooperative binding mid-cycle.
JTJin Tanaka
000
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A 46-residue plant protein resolved at sub-ångström resolution. A tiny but exceptionally well-resolved benchmark for force fields.
Other simulations in the same category.
Human hemoglobin in the oxygen-bound R state. The classic structure that captures cooperative binding mid-cycle.
Human deoxyhemoglobin in the tense T state. Pairs naturally with 1HHO to study the allosteric switch behind cooperative oxygen binding.
The first protein structure ever solved by X-ray crystallography (Kendrew, 1958). Still a benchmark for oxygen-storage dynamics.
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