Editing Protein folding (section)

=== Studies of folding with high time resolution ===
The study of protein folding has been greatly advanced in recent years by the development of fast, time-resolved techniques. Experimenters rapidly trigger the folding of a sample of unfolded protein and observe the resulting [[protein dynamics|dynamics]]. Fast techniques in use include [[neutron scattering]],<ref name="Callaway">{{cite journal | vauthors = Bu Z, Cook J, Callaway DJ | title = Dynamic regimes and correlated structural dynamics in native and denatured alpha-lactalbumin | journal = Journal of Molecular Biology | volume = 312 | issue = 4 | pages = 865–73 | date = September 2001 | pmid = 11575938 | doi = 10.1006/jmbi.2001.5006 }}</ref> ultrafast mixing of solutions, photochemical methods, and [[Temperature jump|laser temperature jump spectroscopy]]. Among the many scientists who have contributed to the development of these techniques are Jeremy Cook, Heinrich Roder, Terry Oas, [[Harry Gray (chemist)|Harry Gray]], [[Martin Gruebele]], Brian Dyer, William Eaton, [[Sheena Radford]], [[Chris Dobson]], [[Alan Fersht]], [[Bengt Nölting]] and Lars Konermann.