Antibodies are proteins produced by the immune system to neutralise pathogens through interactions with their targets, called antigens, and present an attractive avenue for biotherapeutic development. The affinity of an antibody for its antigen is determined by the kinetic profile of the antibody-antigen interaction and two antibodies with the same affinity for their antigens may have vastly different binding and unbinding rates. Even though affinity maturation is often part of antibody lead optimisation, high affinity does not always correlate with neutralising activity. My DPhil project aims to investigate the determinants of binding rates with the aim of providing an in silico tool with which these can be modulated. To experimentally validate my results, I plan to use antibodies effective against <i>Plasmodium falciparum</i> malaria whose neutralising activity has been shown the be highly dependent on binding rates.