Peter Wills

Peter Wills is a theoretical biologist and an Honorary Academic in the Department of Physics at The University of Auckland. His main research focus is on the origin of genetic coding.

His investigations cover theoretical aspects, such as the dynamics of coding self-organisation, computational aspects, such as the phylogeny of the aminoacyl-tRNA synthetase (aaRS) coding enzymes and experimental aspects, such as the de novo reconstruction of aaRS ancestors. Much of this work is conducted in collaboration with Charles Carter of the University of North Carolina at Capel Hill.  Their emphasis on the computational aspects of molecular biology, especially the way organisms use of digitally stored genetic information to synthesise molecular catalysts (protein enzymes), is unique among origin-of-life researchers.  Peter’s first foray into this field was in 1989 when he became a Fellow of the Humboldt Foundation and spent a year in the laboratory of Manfred Eigen at the Max Planck Institute for Biophysical Chemistry in Göttingen, Germany.  With ongoing Humboldt support he has returned for extended periods to work with many other scientists in various German universities (Jena, Bonn, Tübingen, Bochum, Leipzig and Hamburg). Peter began his scientific work in the field of physical biochemistry, studying applications of quasi-elastic light scattering to the investigation of macromolecules in solution. He then branched out into aspects of biophysical theory, especially the thermodynamics and statistical mechanics of macromolecular diffusion, sedimentation and light scattering.  He also investigated theoretical aspects of diseases known as spongiform encephalopathies, and he was recognised by Carleton Gajdusek as an early advocate of the prion hypothesis and subsequently invited to the US National Institutes of Health to pursue his research.  He now has a collaboration with Zoya Ignatova (Hamburg) to conduct experimental investigations into the plausibility of his model of how prions replicate. Throughout his career Peter has been a commentator on issues concerning the relationship of science and society. He was an active participant in debate about weapons of mass destruction during the Cold War and is now involved in discussions about pharmaceutical and agricultural applications of genetic engineering, especially its regulation. This work has often placed him in the public eye, including the relevance of biotechnology to Treaty of Waitangi issues.


Differential equations for error-prone information transfer (template replication, transcription or translation) are developed in order to consider, within the theory of autocatalysis, the advent of coded protein synthesis. Variations of these equations furnish a basis for comparing the plausibility of contrasting scenarios for the emergence of specific tRNA aminoacylation, ultimately by enzymes, and the relationship of this process with the origin of the universal system of molecular biological information processing embodied in the Central Dogma. The hypothetical RNA World does not furnish an adequate basis for explaining how this system came into being, but principles of self-organisation that transcend Darwinian natural selection furnish an unexpectedly robust basis for a rapid, concerted transition to genetic coding from a peptide·RNA world.

Read More

Attention is drawn to the thermodynamic invalidity of the current practice of analyzing static light scattering measurements on globular proteins in terms of theory for a single solute because of its disregard of the need to consider small species such as buffer components as additional cosolutes rather than as part of the solvent. This practice continues despite its demonstrated inadequacy in studies of sucrose-supplemented protein solutions, where the aberrant behavior was recognized to be a consequence of physical protein interaction with the small cosolute. Failure to take into account the consequences of small cosolute effects renders extremely difficult any attempt to obtain a rigorous thermodynamic characterization of protein interactions by this empirical technique.

Read More

Sign up to Our Newsletter