= Max Ferdinand Perutz
{c}
= Max Perutz
{c}
{synonym}
= M. F. Perutz
{c}
{synonym}
\b[<Max Perutz>], fully \b[Max Ferdinand Perutz], investigated protein structure through <X-ray diffraction>. The Nobel nomination archive explicitly pairs his full name with the initials M. F. Perutz and records his 1962 Chemistry prize.<Max Ferdinand Perutz in the Nobel Prize nomination archive>[Nomination Chemistry 1962, number 64-0, nominee name and comment]{ref} His structural research connected the organization of protein atoms with the behavior of oxygen-binding <hemoglobin>.
With <J. A. Frier>, Perutz coauthored the structure of human fetal <deoxyhemoglobin>. The associated primary record, 1FDH, identifies alpha and gamma chains and a diffraction resolution of $2.50\,\mathrm{\mathring A}$.<Structure of human foetal deoxyhaemoglobin by J. A. Frier and M. F. Perutz>[RCSB PDB 1FDH, Literature, Biological Assembly and Experimental Data]{ref} The study relates structural differences to interaction with <2,3-Bisphosphoglycerate>. A structural explanation is strongest when its proposed interaction can also be tested through functional measurements.
An original diffraction example shows why obtaining a molecular structure is not equivalent to photographing atoms directly. In a reduced model, a complex scattering amplitude is
$$
F(q)=\sum_j f_j e^{iqx_j},
$$
where $x_j$ are positions and $f_j$ scattering strengths. Measured intensity is proportional to $|F(q)|^2$. Translating every atom by $x_0$ multiplies $F$ by $e^{iqx_0}$ without changing that intensity. Intensities therefore do not by themselves fix every phase or coordinate convention. Recovering an <electron density> model requires appropriate phase information and structural constraints, connecting the measurement with the <phase problem>.
The fetal structure also illustrates a separate limitation: identifying a deoxygenated conformation does not directly measure the entire oxygen-binding curve. Structural comparisons, ligand-binding experiments and quantitative analysis supply complementary evidence. Perutz's contribution lies in connecting those molecular questions with experimentally determined three-dimensional organization.
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