Foreword to ‘Multiscale structural biology: biophysical principles and mechanisms underlying the action of bio-nanomachines’, a special issue in Honour of Fumio Arisaka’s 70th birthday

Abstract

This issue of Biophysical Reviews, titled 'Multiscale structural biology: biophysical principles and mechanisms underlying the action of bio-nanomachines', is a collection of articles dedicated in honour of Professor Fumio Arisaka's 70th birthday. Initially, working in the fields of haemocyanin and actin filament assembly, Fumio went on to publish important work on the elucidation of structural and functional aspects of T4 phage biology. As his career has transitioned levels of complexity from proteins (hemocyanin) to large protein complexes (actin) to even more massive bio-nanomachinery (phage), it is fitting that the subject of this special issue is similarly reflective of his multiscale approach to structural biology. This festschrift contains articles spanning biophysical structure and function from the bio-molecular through to the bio-nanomachine level.

On the nature of the optimal form of the holdase‐type chaperone stress response

“…17 With regards to the description of the foldable protein pool, the assumption that all proteins can be considered as soluble monomers exhibiting two-state folding behaviour neglects the fact that proteins can (a) exist in complexed form e.g. from simple dimers to components in huge multi-subunit biological machines [104]; (b) may be obligate membrane proteins, peripherally or integrally located, and therefore follow a temperature unfolding profile different from that exhibited by proteins normally resident in solution space [105]; and (c) may not display two-state folding behaviour, typically the case as proteins become larger [106]. Recognizing that all of the preceding points are true, does not fundamentally detract from the basic veracity of our model but rather adds to it.…”