Personal Statement - Biochemistry 10

Biochemistry Personal Statement 10

In the sciences, every answer raises a new question. The field is one of infinite possibility and this is what most attracts me to it. Studying biochemistry would allow me to understand in detail the complexity of life and how different systems within it interact. To me, it explains the beauty of life, how it can be broken down into various chemical reactions and by studying the chemical composition and structure of separate biological molecules, I hope to gain a more cohesive understanding of life.

I was fortunate to arrange work experience at the Wellcome Trust Centre for Human Genetics. I was able to observe and take part in practical tasks such as running a PCR and to learn the importance of meticulous experimental design and analysis of data. I was encouraged to ask questions of the researchers in the laboratory: their commitment and patient determination were infectious. A subsequent visit to a chemistry lab at the University of Oxford confirmed for me that this is the kind of work that I want to be doing.

Being naturally inquisitive, when my chemistry teacher mentioned that amino acids in the body are exclusively left-handed, I set out to learn why. After extensive research I was excited to discover that it has not yet been definitively answered. I was particularly interested to learn that the left-handedness challenges evolutionary theory and felt compelled to explore further. I was surprised by the ambiguity surrounding abiogenesis: the more I discovered, the more unanswered questions I found. By reflecting on this I learnt the exciting consequence of asking a good question -- it leads to another.

This experience (and an article in Scientific American magazine) inspired me to design an experiment with a group of friends for the school science fair in which we found out how and why illusions affect different people to varying degrees and whether those variations are attributable to a person’s genetic makeup or to their environment. This led me to Matt Ridley’s ‘Nature via Nurture,’ which shed much light on the subject, and introduced me to the idea that nature and nurture are not opposing factors but, rather, interactive. It explained concepts such as alternative splicing, revealing how the same genes can encode multiple proteins and so can account for life’s complexity. I feel that the idea needs to be explored further, and the mechanisms of the interactions studied more closely. I am excited by the possibility that this could lead to a better understanding of the nature of personality, which in turn may help us to understand and treat its disorders.

I have also enjoyed the challenge of mathematics, particularly the difficulty of abstract reasoning and logical problem-solving, both relevant for much of my work in chemistry. I strongly believe in the importance of sharing ideas to progress, so aspire to build upon my language base by spending my gap year in Syria learning Arabic as well as taking one year Open University course in Mandarin Chinese. Furthermore, studying piano and flute for many years has undoubtedly required self-discipline, patience and perseverance. Participating in the Peer Support program at school has contributed a lot to my interpersonal skills and confidence, particularly helping me improve my clarity of expression.

Biochemistry combines the best of what I have found most challenging and rewarding in the different subjects I have studied. I am certain that it is what I want to specialise in and am confident that my curiosity and determination will help me do so.


Universities Applied to:

  • Oxford University (Biochemistry) - Offer (AAAa) Firm
  • Cardiff University (Biochemistry - biomedical route) - Offer (ABB) Insurance
  • Imperial College London (Biochemistry with French) - Offer (AAAb) Rejected
  • Nottingham University (Biochemistry) - Offer (AAB) Rejected
  • Bath University (Biochemistry) - Offer (AAB) Rejected

Grades Achieved:

  • Chemistry (A2) - A
  • Biology (AS) - A
  • Maths (A2) - A
  • French (A2) - A