Welcome back to the Deep Dive. Today we are opening
the file on a scientist whose career, well, it
wasn't really defined by a single flash of genius,
but by something much rarer. 35 years of relentless,
methodical patience. Exactly. We're diving into
the atomic architecture of life itself. And we're
following the trajectory of Dorothy Crowfoot
Hodgkin. We're examining the sources surrounding
the life and the profound work of Dorothy Hodgkin.
She was born in 1910. And, you know, she remains
the only British woman scientist to win the Nobel
Prize in chemistry. Which she won in 1964. That's
right. And the material we've gathered really
illustrates a career just dead. dedicated to
transforming this one technique, x -ray crystallography,
from a sort of theoretical curiosity into the
essential method for structural biology. Okay,
let's unpack that. Our mission here is to really
get to grips with how a scientist who is often
working through a debilitating illness and navigating
I mean, intense Cold War political tensions.
How she managed to map the precise three -dimensional
structures of penicillin, vitamin B12, and then
the big one, insulin. She didn't just study molecules.
She gave us the blueprints to life -saving medicine.
That phrase, blueprints to life -saving medicine,
is exactly it. It's perfect. But before we can
even begin to appreciate the scale of her molecular
conquest, we have to establish the... the battlefield
so to speak the technique it's a technique everything
hodgkin achieved relied on her mastery of x -ray
crystallography a technique so complex that it
took her over three decades and frankly the invention
of modern computers to fully realize its potential
So let's nail this down first because it really
is the foundation of her entire legacy. We know
the basics. You shoot x -rays at crystals. A
pattern is created. But for an audience that
gets the fundamentals of chemistry, what was
the technical hurdle that made applying this
to complex biological stuff so revolutionary?
Well, the initial hurdle wasn't really about
collecting the x -ray data. That part was, I
mean, difficult but understood. It was the interpretation.
It was all about interpretation. When x -rays
hit the regularly arranged atoms inside a crystal,
they scatter or diffract. In this diffraction
pattern, it looks like a series of spots on a
piece of photographic film. Now, the intensity
of those spots, how bright they are in their
location, that contains all the information about
where every single atom is. So the pattern is
the key. But how on earth do you go from a flat
two -dimensional pattern of dots to a, you know,
a three -dimensional model of a hugely complex
molecule like a protein? That's the million -dollar
question. And it requires the most challenging
step in crystallography, which is solving what's
known as the phase problem. The phase problem.
Right. When light, or in this case x -rays, is
scattered, you can measure the intensity of the
scattered waves. You can see how bright the spot
is. Okay. But you lose the information about
the phase of that wave. And the phase is... Essentially,
it's the timing or the starting point of that
wave relative to all the others. So without the
phase, you have all the ingredients, but you
have absolutely no recipe for how to assemble
the molecule. Exactly. You said it perfectly.
Mathematically, to reconstruct the electron cloud
of the molecule, you have to sum up a whole series
of waves. It's a process called a Fourier transform.
Right. But if you don't know the phase of those
waves, the resulting map is just... It's garbage.
It's meaningless. And Hodgkin's genius, her real
contribution, lay in finding clever ways to determine
or at least estimate those phases for bigger
and bigger molecules. And the result of that
is these three -dimensional contour maps of electron
density. Yes, which allow you to pinpoint exactly
where the atoms are sitting. This is why her
work was so essential. She didn't invent crystallography,
but you could say she invented the methods that
made it work for biology. That sets the stage
perfectly. She was dealing with a structural
problem, a mathematical problem, and a computational
problem all at once. And a personal one, as we'll
see. Let's move into part one then. The Architect
of Atoms. Her early life and influences, because
it really seems like her formative years instilled
the exact kind of detailed pattern recognition
she would need later on. Absolutely. Dorothy
Mary Crowfoot was born in Cairo, Egypt in 1910.
Her parents, John Winter Crowfoot and Grace Mary
Hood, everyone called her Molly. They were deeply
involved in colonial administration and later.
So they were based in North Africa and the Middle
East. Yes, which meant her childhood was, to
say the least, unusual. Nomadic, really. The
sources say she spent a lot of her early years
separated from her parents, staying with her
grandparents near Worthing in England. That sounds
quite isolating. It could have been, but the
sources suggest a very strong intellectual influence,
especially from her mother, Molly. Okay, tell
me about Molly. Molly was a very proficient,
dedicated botanist, and she really fostered Dorothy's
innate curiosity. She didn't just, you know,
encourage an interest in science. She provided
the critical early tools. At age 10, Dorothy
was already fascinated by crystals. She was growing
them. And then for her 16th birthday, Molly gave
her a copy of W .H. Bragg's seminal work concerning
the nature of things. And Bragg, of course, was
one of the absolute pioneers of X -ray diffraction.
So that gift wasn't just a book. It was a roadmap.
It was a signpost. It solidified her career path
almost instantly. She wrote about it years later,
about the clarity of that moment. But before
she fully committed to chemistry and X -ray analysis,
there was this fascinating detour. Into archaeology.
Yes, which if you look at it structurally, it
looks exactly like her later scientific work.
It's incredible. Tell us about that. This feels
like a real key to understanding her mind. Well,
in 1928, at the age of 18, Hodgkin went to join
her parents at an archaeological site. It was
Jerash, in what is now Jordan. The site was filled
with ancient Roman and Byzantine ruins. And what
was her job there? Her job was incredibly rigorous.
She was tasked with documenting the Byzantine
era mosaics from these fifth and sixth century
churches. And these things are just incredibly
intricate. So she was essentially performing
a kind of pre -chemical structural analysis.
Precisely. She spent over a year creating these
precise, measured scale drawings of incredibly
complex and often fragmented floor patterns.
Piece by piece. Piece by piece. Tessera by tessera.
It requires an intense, almost obsessive focus
on pattern. on detail, on symmetry, and on reconstruction
from partial data. She was decoding the blueprint
of ancient stones. Yes, which required the exact
same mental muscle she would later use to decode
electron density maps. She even did chemical
analyses on the little glass tesserae to understand
their composition. The sources say she enjoyed
it so much, she actually considered switching
to archaeology for good. That's a profound thought,
isn't it? The greatest structural chemist of
her generation almost became an archaeologist.
It's an amazing sliding doors moment. But thankfully
for science, she stepped with chemistry, though
she still had to overcome these early institutional
barriers. Right. The entry requirements for university.
She did. Her school, the Sir John Lehman Grammar
School, it didn't teach Latin. And back then,
Latin was a non -negotiable requirement for getting
into Oxford or Cambridge. So what did she do?
Her headmaster had to personally give her private
Latin tuition so she could pass the entrance
exam. It just highlights how arbitrary and frankly
gendered the hurdles were for aspiring female
scientists at that time. But she cleared them.
She got into Somerville College at Oxford in
1928 and graduated in 1932 with a first class
honors degree in chemistry. And she was one of
only three women at the institution to achieve
that distinction at the time. A huge achievement.
But the real scientific revolution for her started
when she left Oxford. When she went to Cambridge.
That's right. She immediately went to Cambridge
to start her Ph .D. at Newnham College under
a man named John Desmond Bernal. He was often
known simply as the sage. And Bernal wasn't just
your supervisor, was he? No. He was a catalyst
for her entire worldview, scientifically, politically,
and personally. They were lovers for a time before
her marriage. So how deep was his influence and
why was he so pivotal for her research? Bernal...
was a visionary he was one of the few people
who believed that x -ray crystallography could
be applied not just to simple salts or minerals
but to the massive complicated machinery of life
itself proteins which was a very controversial
idea at the time most people thought proteins
were just biological sludge A lot of chemists
did, yes. They thought they were too irregular,
too amorphous to ever form crystals suitable
for X -ray diffraction. Bernal thought differently.
He did. And Hodgkin worked with him on the technique's
very first application to a crystalline protein,
pepsin. Pepsin's a digestive enzyme. Bernal took
the initial, very rough X -ray photographs. And
what did those first pictures show? They showed
spots. Clear, defined diffraction spots. This
was a moment of utter revelation. It proved they
weren't just goo. It proved definitively that
protein molecules were orderly, three -dimensional
structures with repeating internal patterns.
They weren't amorphous at all. Hodgkin is credited
with extending this foundational work, and that
moment, the pepsin experiment, that was a birth
certificate of structural biology as a discipline.
It's incredible. She was there at the very beginning
of the field she would later come to dominate.
And yet she eventually returned to Oxford, which
became her scientific home for the rest of her
life. She did. In 1933, she was awarded a research
fellowship by Somerville College. She went back
the next year, set up a small lab, started teaching
chemistry. And by 1936, she was appointed the
college's first fellow and tutor in chemistry,
a position she held for over 40 years. That stability
must have been crucial. It was. That stability
at Oxford allowed her to focus on the long, decade
-spanning projects that would come to define
her entire career. And before we leave this crucial
period, we have to acknowledge this really unlikely
academic connection she forged in the 1940s,
a relationship that crosses the, well, the great
political chasm of modern Britain. It's one of
the great historical footnotes, isn't it? Margaret
Roberts. Who would later become Margaret Thatcher.
That's the one. She was Hodgkin's undergraduate
student from 1943 to 1947, and Hodgkin had a
profound effect on Thatcher's scientific training.
The ultimate Tory prime minister learning chemistry
from a committed, lifelong socialist. What does
that tell us about their professional dynamic?
I think it speaks volumes about mutual respect
in the pursuit of knowledge. Hodgkin was a lifelong
Labor Party supporter. Her husband was even in
the Communist Party for a while. And Thatcher,
well, she became the figurehead of modern conservatives.
That complete political opposition. And yet Thatcher
held Hodgkin in such high regard that years later
she commissioned a portrait of her. and hung
it prominently in her Downing Street office.
Wow. They may have disagreed fundamentally on
how society should be governed, but they absolutely
agreed on the fundamental rigor of science. It's
a powerful testament to the idea that scientific
truth can sometimes transcend political ideology.
That sets the stage perfectly for the paradoxes
in her later life, which we'll get to when we
cover her peace activism. But first, let's jump
into the actual core breakthroughs. Part two,
the core discoveries, charting the path from
steroids to the Nobel Prize. Her journey really
began with her PhD research on sterols, which
are a class of steroids. After she earned her
PhD in 1937, she just kept going with this work.
And by 1945, working very closely with C .H.,
Harry Carlyle, she achieved her first major structural
success. Which was the structure of cholesterol
iodide. That's it. So why was that particular
structure so important? Because it was the first
ever three -dimensional biomolecular structure
of a steroid determined using X -ray. crystallography.
Steroids are these complex, bulky molecules,
you know, hormones like testosterone, cholesterol.
Right. And successfully mapping the full 3D geometry
of one of them demonstrated to the entire scientific
community that X -ray crystallography was a viable
tool for complex organic compounds. It proved
the method had graduated from simple salts to,
you know, biologically relevant molecules. And
the very next molecule she tackled was immediately
relevant to the global conflict that was underway
at the time, penicillin. The urgency couldn't
have been higher. This was during World War II.
The life -saving potential of penicillin was
obvious, but to manufacture it, to modify it,
you had to know its exact structure. It became
a critical, highly secretive wartime project.
It did in 1945. And Hodgkin and her team, which
notably included a brilliant scientist named
Barbara Lowe, they were the ones who solved the
structure. Now, this is where this specific chemical
detail really matters. Why was the structure
so hotly debated? And what did Hodgkin's crystallography
reveal that finally settled the argument? Well,
the scientific community, especially the synthetic
organic chemists, they were completely split.
The two main proposed structures for penicillin
had fundamentally different cores. One involved
a simple thiazolidine ring structure, but the
other one, which was supported by Hodgkin's data,
contained this four -membered, highly reactive
structure called a baloctam ring. And why was
that so common? Because the ball -lactam ring
is chemically unstable. It's strained, it's reactive,
which is precisely why penicillin works. That
reactivity is what lets it attack bacterial cell
walls and interrupt their synthesis. Hodgkin's
structural map confirmed the presence of this
unstable ring, and in doing so, it proved the
structural model championed by Robert Robinson,
who had actually been an initial skeptic. So
she provided the definitive proof. The structural
key that told synthetic chemists exactly what
they needed to recreate and eventually modify
to produce newer generations of antibiotics.
That's it. Without knowing that precise spatial
arrangement, large -scale synthesis would have
been impossible, or at the very least far, far
less efficient. And the work was completed in
1945. It was, but because of the wartime secrecy
and just the massive amount of data, the full
publication didn't appear until 1949. And notably,
it was published under her maiden name, Dee Crowfoot.
It's incredible to think that the core chemical
secret of the world's first widely successful
antibiotic was delivered by her team. And if
penicillin was groundbreaking, the next target,
vitamin B12, was her Everest. It truly was her
structural Everest. This is the work that earned
her the Nobel Prize, and it was a technical leap
that Lawrence Bragg famously compared to breaking
the sound barrier. She started on B12, or cobalamin,
in 1948. So why was vitamin B12 so uniquely difficult?
What made it a sound barrier moment? B12 was,
by a huge margin, the largest, most structurally
complex vitamin known at the time. How big are
we talking? We're talking a tangled knot of 181
atoms, a massive biological structure compared
to penicillin. And most critically, previous
attempts to solve the phase problem for molecules
of this size had just completely failed. The
computational power simply did not exist to process
the hundreds of thousands of individual X -ray
reflections. So the sheer size and the complexity
were the immediate barriers. How did she bypass
the phase problem for this monster of a molecule?
This is where her genius for methodological innovation
really shone through. She had a flash of insight.
She realized the molecule contained a single
heavy metal atom. Cobalt. The cobalt clue. Precisely.
Compared to all the light atoms that make up
the rest of the molecule, you know, carbon, nitrogen,
hydrogen, the cobalt atom, with its high electron
count, it scatters X -rays much, much more strongly.
And she used that to her advantage. She used
it to employ what's now called the heavy atom
method. Can you elaborate on that method? Sure.
A heavy atom acts like a fixed reference point.
A massive beacon inside the crystal. Because
the scattering contribution of that single heavy
atom is so dominant, you can calculate its position
relatively easily. I see. And once you know the
exact phase contribution of that one atom, you
can use some complex mathematics to estimate
the phases of all the rest of the scattered X
-ray waves. It effectively solves the phase problem
for the entire structure. That's a profound shift
in using a chemical feature of the molecule to
solve a purely mathematical problem. it turns
a limitation into a huge opportunity. It was
absolutely revolutionary. It proved that even
massive biological structures could be forced
to yield their secrets. Now, the work took years
of painstaking measurement and calculation, often
relying on these early punch card computing systems.
A dawn of computing. It was. But the final resolved
structure published in 1955 and 1956 was just
unprecedented. And it was this detailed three
-dimensional blueprint of B12 that led directly
to her Nobel Prize in Chemistry in 1964. This
ability to map structures provides the blueprint
not just for understanding function but for chemical
synthesis. It fundamentally changed how we approach
complex pharmaceuticals. Which brings us perfectly
to the next and longest chapter of her life.
the quest for insulin. Ah, the 35 -year quest
for insulin. This is the defining narrative of
her entire career's tenacity. She received her
first sample of crystalline insulin from Robert
Robinson way, way back in 1934. 1934. Yes. And
the fascination for her was immediate because
of the hormone's profound and complex effect
on human metabolism and its direct link to diabetes.
25 years. That's a career within a career. I
mean, if she had solved B12 by 1956, Why did
insulin remain unconquerable for another decade
and a half? It was pure complexity and computational
limitation. Insulin is a small protein. It's
made up of 51 amino acids, and they form this
complex structure with two linked chains. So
it's much bigger than B12. B12 had 181 atoms.
Insulin has many hundreds more, especially when
you factor in all the solvent molecules in the
crystal. This complexity just created an impossibly
dense electron cloud. The math required... to
perform that Fourier transform on insulin must
have been astronomical. It was beyond manual
calculation. I mean, in the 1930s, crystallographers
used these things called Beaver's Lips and Strips.
They were small, pre -calculated Fourier coefficients
to help perform the sums. A kind of manual calculator.
Exactly. But even for a molecule of insulin size,
you would need to perform millions of these sums
by hand. It just wasn't feasible. They had the
method, but they had to wait for the technology
to mature. So the true breakthrough in 1969 wasn't
some sudden chemical insight, but rather the
necessary symbiosis between fundamental science
and technological advancement. The arrival of
high -speed digital computing. Absolutely. The
mid to late 1960s saw that necessary leap in
computing power and also refinement of the X
-ray techniques themselves. This finally allowed
Hodgkin and her large international team to tackle
the mountain of calculations required to solve
the phase problem and generate the accurate electron
density maps. And in 1969, they did it. By 1969,
they published the 3D structure of the insulin
hexamer. The quest was over. And the impact of
finally having that blueprint must have been
enormous for diabetes research. It was instrumental
on two major fronts. First, just understanding
the structure allowed pharmaceutical companies
to refine their methods for the mass production
of naturally derived insulin. But second, and
far more critical in the long run, the structure
provided the precise location of every single
atom. Scientists could then rationally alter
the molecule structure. They could mutate amino
acids or change the crystallization solvent to
create improved drug options. Like longer acting
or faster acting insulins. Exactly. For both
type 1 and type 2 diabetes patients. She continued
to work on this, advising laboratories all over
the world, cementing her commitment to the real
world application of structural science. For
science was never siloed, was it? And that brings
us naturally to the profound and sometimes challenging
political dimensions of her life. Indeed. We've
already established her lifelong commitment to
the Labor Party, which contrasted so sharply
with her famous former student Margaret Thatcher.
But the political environment she operated in,
particularly during the Cold War, placed her
in frequent conflict with Western governments.
And her husband, Thomas Hodgkin, he was an eminent
historian. He was part of this narrative as well.
Thomas was an intermittent member of the Communist
Party. He spent significant time abroad, particularly
in West Africa, advising figures like Ghana's
President Kwame Nkrumah. And that association,
combined with Dorothy's own deeply held beliefs
about peace and social equality, drew the suspicion
of U .S. authorities. It did. And this suspicion
had very real, punitive consequences for her
scientific life. Oh, absolutely. Due to her political
activities and her husband's associations, the
U .S. government banned her from entering the
country in 1953. 1953. Imagine that. A scientist
on the absolute cusp of the B -12 breakthrough
barred from attending essential international
conferences. For subsequent visits, she was only
granted entry through a special CIA waiver. That
puts into sharp relief the challenges faced by
scientists trying to maintain international collaboration
during the height of the Cold War. She was, in
effect, a scientific bridge builder operating
under continuous surveillance. That's the perfect
description. Hodgkin deliberately and actively
maintained her scientific contacts across the
Iron Curtain. She had deep connections with crystallographers
at the Institute of Crystallography in Moscow.
She visited India regularly, and she established
a really powerful relationship with a Chinese
group who were also working on insulin. How often
did she go to China? She visited China seven
times between 1959 and 1993. That takes some
serious commitment. especially given the geopolitical
climate of the time. Her commitment to global
science was unwavering. There is a particularly
powerful anecdote from 1971. The Chinese group,
who had been working in complete isolation, they
had independently solved the structure of insulin.
Wow. And for a moment, they'd achieved a resolution
even higher than Hodgkin's own team. And Hodgkin,
she recognized the brilliance of their achievement
and worked tirelessly to try and integrate them
into the global scientific community. But the
political barrier... were just too high, even
for a Nobel laureate. She served as president
of the International Union of Crystallography
from 1972 to 75, but she was unable to persuade
the political authorities in China to allow their
scientists to become members of the union or
to attend its international meetings. So the
data was shared. But the human connection was
restricted. It was. It really shows the limits
of science as a diplomatic tool when it's faced
with hard state policy. And her motivation for
all this, it was clearly fueled by the social
conscience she inherited from her mother. That
social conscience drove her profound concern
about social inequalities and increasingly the
devastating threat of nuclear war. This led her
into what was really a major second career in
peace activism. As president of the Pugwash Conferences.
She served as president of the Pugwash Conference
on Science and World Affairs from 1976 all the
way to 1988. And the Pugwash conferences were
crucial for bringing scientists from East and
West together to discuss arms control. Her leadership
there must have been incredibly valuable, given
her established connections in Moscow and Beijing.
Her integrity gave her credibility across all
ideological lines. Her dedication to peace and
disarmament was recognized in 1987 when she accepted
the Lenin Peace Prize from the Soviet government.
That's a significant honor. It was, and it came
just a year before the signing of the Intermediate
-Range Nuclear Forces Treaty, which dramatically
reduced the risk of nuclear confrontation in
Europe. We should also briefly touch upon one
highly unusual political entanglement that sort
of underscores the risk of operating in these
politically charged environments. The anecdote
involving the Romanian dictator's wife. It's
a layer of nuance that highlights the, well,
the fraught reality of international scientific
diplomacy. In her early 70s, Hodgkin agreed to
write a foreword for an English edition of a
scientific book. What was the book? It was titled
Stereospecific Polymerization of Isoprene, and
the book was published as the work of Elena Sulescu,
the wife of Romania's communist dictator, Nicolae
Hiescu. Hodgkin wrote positively about the author's
outstanding achievements. But the reality was
far less savory. Much less. After the overthrow
of the Sayasu regime in 1989, it was completely
exposed that Elena Sayasu's scientific credentials
were entirely fraudulent. The work was ghostwritten
for her by others. So Hodgkin was used. It was
an incident that illustrated how political figures
sometimes exploit the credibility of true scientists
like Hodgkin for legitimacy. She was ultimately
a brilliant but perhaps, you know, politically
naive diplomat who just believed in universal
human contact. It shows that even the most grounded
scientists can get caught up in the machinations
of global politics. Now let's pivot sharply to
part four, resilience and recognition, because
all these monumental achievements, the decades
of calculation, the global travel, the political
maneuvering, they were all accomplished while
she battled a crippling physical adversary. This
is perhaps the most humbling part of her story,
her battle with rheumatoid arthritis. She was
diagnosed at just 24 years old in 1934. The condition
caused immense pain. aggressive swelling, and
eventually distortion in her hands and feet.
For a scientist whose entire life was defined
by the precise manipulation of delicate crystals,
fine instruments, and careful positioning of
x -ray cameras, that diagnosis must have been
just... It was an immediate physical obstacle
to her work. The sources recount this particularly
powerful, almost poignant image of her in the
lab. What was that? Due to the increasing stiffness
and deformity of her hands, she struggled to
operate the main electrical switch on the x -ray
equipment, a simple action that you'd need to
do countless times a day. And what did she do?
She didn't stop. Instead of abandoning the work,
she improvised. She constructed a specific lever
mechanism that allowed her to operate the switch
using her shoulder or forearm, compensating for
the lack of fine motor control in her hands.
That image, the future Nobel laureate having
to engineer a tool just to operate the tool that
would unlock the structures of life, it's a symbol
of her fierce determination. Her condition continued
to worsen over time, didn't it, leading to severe
deformities and the necessity of using a wheelchair
in her later years. And yet her scientific output
never ceased. Her persistence was absolute. She
remained scientifically active, traveling the
globe, mentoring students right up until her
death in 1994. Her personal story of resilience
is just inextricably linked to her scientific
accomplishments. That incredible persistence
was naturally matched by the magnitude of the
honors she received. They truly reflected her
global and historical impact. The Nobel Prize
in Chemistry in 1964 for her work on vitamin
B12 was, of course, the highest possible scientific
honor. But the recognition went far beyond the
academic community. In 1965, she was appointed
to the Order of Merit. Which is a very rare personal
distinction granted by the reigning British monarch
for exceptional service. She was only the second
woman ever to receive it. And she broke another
significant gender barrier at the Royal Society
later on. She did. In 1976, she became the first
woman ever to receive the prestigious Copley
Medal from the Royal Society, a highly respected
award established way back in 1731. That's a
big deal. It recognized her overall achievement
in structural biology and placed her in the company
of historical giants like Darwin and Einstein.
She accumulated a long list of other major honors
as well, didn't she? Absolutely. The Royal Medal
in 1956, the Lomonosov Gold Medal from the Soviet
Academy of Sciences in 1982, the Dalton Medal
in 1981. The list goes on. Institutionally, she
also served as chancellor of the University of
Bristol from 1970 to 1988. And circling back
to the Royal Society. Right. In 1982, she was
the first woman fellow of the society to have
her portrait included in their permanent collection.
Let's talk about her nomenclature for a second
because her various names, Crowfoot, Crowfoot
Hodgkin, Hodgkin, they reflect the historical
changes in how professional women were recognized
at the time. It's a fascinating historical marker.
Initially, she published exclusively as Dorothy
Crowfoot. It wasn't until 1949, 12 years after
her marriage, that she was persuaded to include
her married name for her contribution to a book
chapter on penicillin. And today. Today, different
institutions use slightly different names. The
Royal Society's celebrated fellowship is just
named the Dorothy Hodgkin Fellowship, while others,
like the National Archives, use her full maiden
and married names. Dorothy Mary Crowfoot Hodgkin.
It shows the complex transition in professional
identity for women marrying during that era.
But her most enduring legacy is perhaps not in
the names on awards or publications, but in the
institutional support she inspired for future
scientists who are facing similar hurdles. That
is the most profound part of her influence, I
think. The Royal Society's Dorothy Hodgkin Fellowship
is designed specifically to support outstanding
early career scientists who require a flexible
working pattern due to personal circumstances.
So things like parenting or caring responsibilities.
Or, most poignantly, health -related reasons.
It recognizes that brilliant science doesn't
happen in a vacuum of perfect health or domestic
support. It institutionalizes the recognition
of the exact barriers she had to navigate throughout
her entire life. It ensures that her legacy is
not just about the molecules she mapped, but
about the conditions under which structural science
can thrive for everyone. And finally, Britain
has commemorated her twice on stamps, placing
her alongside true scientific titans. In 1996,
as one of five women of achievement, and then
again in 2010. Yes, and the 2010 set was particularly
significant. It was celebrating the Royal Society's
350th anniversary, and she was the only woman
featured in a set of 10 stamps honoring the society's
most illustrious members. Placing her permanently
alongside figures like Isaac Newton, Robert Boyle,
and Ernest Rutherford. A remarkable testament
to a truly impactful life. So what does this
all mean? Our deep dive into Dorothy Hodgkin
reveals a scientist whose genius, I think. really
lay in her structural patience and her methodological
innovation. She took X -ray crystallography and
by overcoming the mathematical and the computational
limitations. From the heavy atom method on B12
to waiting decades for computers to be able to
solve insulin. Right. She provided the essential
blueprints for these life -saving molecules.
And she did all of this while navigating a crippling
illness and the treacherous ideological lines
of the Cold War. Her 35 -year pursuit of insulin
is the ultimate lesson, isn't it? She began with
a question in 1934 that was, for all intents
and purposes, technically unsolvable. The solution
was unlocked in 1969, not by a sudden change
in chemical understanding, but by the relentless
refinement of technique coupled with the arrival
of necessary computational power. It was a victory
of enduring vision and really faith in technology.
It was. And that leads us to our final provocative
thought for you, the listener. Hodgkin showed
us that the greatest breakthroughs sometimes
require not just genius, but the humility to
wait decades for technology to catch up to the
theoretical ambition. So, which major biomedical
breakthrough today? Perhaps understanding the
precise, ultra -high -resolution structure of
a misfolding protein implicated in Alzheimer's
or Parkinson's, or modeling the exact dynamics
of large viral complexes? Which one is currently
stalled by technical limits, just waiting for
a modern 35 -year quest of patience and computational
dedication to unlock its secret? Something to
consider as you digest this knowledge. Thank
you for joining us for the Deep Dive. We'll see
you next time.