Perhaps
being accepted into
graduate school for physics at the tender age of
19 was a clear indication that Prof. Venkatraman
Ramak r i shnan was des t i ned for g reatnes s .
Convinced that he had chosen the wrong field
half way through his Ph.D. and unable to see
what the future in physics held in store for him, he
made the difficult decision to switch to biology
after already obtaining his Ph.D. in physics – a
field that seemed to mimic the exciting phase
that physics was in, in the first part of the 20th
century. He returned to graduate school to learn
biology from the basics, leaving behind all shreds
of the arrogance of a physicist but retaining the
translatable knowledge he had gathered as an
applied physicist to his new field.
After his switch to biological studies, Prof.
Ramak r i shnan fami l iar i sed h imsel f with the
r ibosome. The r ibosome was f i r s t obser ved
under an electron microscope in the 1950s by
cell biologist George Emil Palade. However,
its cellular role was not well understood at the
time. A cell organelle universal to bacter ia,
eukaryotes and mitochondria, the ribosome has
the fundamental role in deciphering translation
of genetic information to create proteins. In
addition to reading RNA, ribosomes also have the
vital task of linking amino acids together – what
The Ribosome with
Prof.
Venkatraman
Ramakrishnan
By Cherry Chow
周卓瑩
核糖體
—
文卡特拉曼．拉馬克裡斯南
教授
was previously thought by some biologists to be
the result of proteins linking themselves. Merely a
speculation for decades, the result of solving the
structure of the ribosome confirms its essential role
in protein synthesis. In Prof. Ramakrishnan’s own
words, it is the building block essential to all of life;
and everything made in a cell is either made by
the ribosome or by enzymes that themselves were
made by the ribosome.
The road to deciphering the ribosome was
not one without tribulations. Ribosomal structure
consists of a large and small subunit that fit
together in operation. Prof. Ramakrishnan and
his team were able to obtain cr ystals of the
ribosome subunit but not of the small subunit. To
complicate matters, the crystals were prone to
radiation damage from their methods, and larger
than anything that they had solved previously.
In addition, trapping the entire ribosome in its
precise functional state was an arduous and time-
consuming process. However, their perseverance
paid off.
2009 marked the year that Prof. Ramakrishnan
was jointly awarded the Nobel Prize in Chemistry
with Thomas A. Steitz and Ada E. Yonath for their
work in mapping the structure and function of
the ribosome, and decoding the processes at
the atomic level. Their critical role in the synthesis
of proteins is essential to life. Not only are they
important nutrients that help build muscle, but
they are the molecules responsible for almost
every molecular action in the human body. From
haemoglobin that circulates in blood, to insulin
that regulates the body’s glucose levels. The
