It has become widely accepted that many phase transitions do not follow nucleation pathways as envisaged by the Classical Nucleation Theory. Many substances can traverse intermediate states before arriving at the stable phase. In this talk we will discuss the nucleation of the protein glucose isomerase that follows a classical pathway in two dimensions and has all the characteristic of a two-step mechanism in three dimensions. Molecular resolution atomic force microscopy imaging of the two-dimensional nucleation of glucose isomerase demonstrates that the interior of subcritical clusters is in the same state as the crystalline bulk phase and that glucose isomerase 2D crystals are formed classically. Our observations illustrate the resurfacing importance of the classical nucleation theory by re-validating some of the key assumptions that have been recently questioned.
In contrast, according to the two-step mechanism of nucleation, protein-rich clusters serve as locations for and precursors to the nucleation of protein crystals. We will report on our characterization of these mysterious clusters with Brownian microscopy. Using confocal Depolarized Dynamic Light scattering we were able to follow nuclei at birth.
Original languageEnglish
Publication statusPublished - 2017
Event21st American Conference on Crystal Growth and Epitaxy - Santa Fe, NM, United States
Duration: 30 Jul 20174 Aug 2017

Conference

Conference21st American Conference on Crystal Growth and Epitaxy
Abbreviated title(ACCGE2-21)
CountryUnited States
CitySanta Fe, NM
Period30/07/174/08/17

ID: 30582865