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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Human deoxyhemoglobin in the tense T state. Pairs naturally with 1HHO to study the allosteric switch behind cooperative oxygen binding.
Other simulations in Globins.
Human hemoglobin in the oxygen-bound R state. The classic structure that captures cooperative binding mid-cycle.
The first protein structure ever solved by X-ray crystallography (Kendrew, 1958). Still a benchmark for oxygen-storage dynamics.
Small, exceptionally stable Kunitz-domain inhibitor of serine proteases — one of the most thoroughly studied proteins in biophysics.
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