He shared the 2009 Nobel Prize in Chemistry with Thomas A. Steitz and Ada Yonath for research on the structure and function of ribosomes.

[23] Ramakrishnan moved to Vadodara (previously also known as Baroda) in Gujarat at the age of three, where he had his entire schooling at the Convent of Jesus and Mary, except for a year and a half (1960–61) which he and his family spent in Adelaide, Australia.

[1] Immediately after graduation he moved to the US, where he obtained his Doctor of Philosophy degree in physics from Ohio University in 1976 for research into the ferroelectric phase transition of potassium dihydrogen phosphate (KDP)[24] supervised by Tomoyasu Tanaka.

[38][39][40] Ramakrishnan's term as president of the Royal Society from 2015-2020 was dominated by Brexit and, in his final year, the COVID-19 pandemic and its response.

Ramakrishnan wrote, "A deal on science is in the best interests of Europe as a whole and should not be sacrificed as collateral damage over disagreements on other issues.

If we are going to successfully tackle global problems like climate change, human disease and food security, we can't do so in isolation.

In 2007, Ramakrishnan was awarded the Louis-Jeantet Prize for Medicine[7] and the Datta Lectureship and Medal of the Federation of European Biochemical Societies (FEBS).

His certificate of election to the Royal Society reads: Ramakrishnan is internationally recognised for determination of the atomic structure of the 30S ribosomal subunit.

Earlier he mapped the arrangement of proteins in the 30S subunit by neutron diffraction and solved X-ray structures of individual components and their RNA complexes.

The RNA interactions representing the P-site tRNA and the mRNA binding site were identified and the likely modes of action of many clinically important antibiotics determined.

His most recent work goes to the heart of the decoding mechanism showing the 30S subunit complexed with poly-U mRNA and the stem-loop of the cognate phenylalanine tRNA.

He has also made substantial contributions to understanding how chromatin is organised, particularly the structure of linker histones and their role in higher order folding.