There are hundreds of articles on this topic. This review is a good place to start. A backward search on some of the early references in the review will bring up most of the papers on the topic.

http://www.ncbi.nlm.nih.gov/pubmed/14499926

Oh excellent, I was searching the exact phrase and it was looking like a niche topic (just a couple of Food Biochem. textbooks). I asked over on r/biophysics and didn't get much positive feedback so was worried I was right.

Thanks Jeffrey, that'll be great for a starting point.

Just as a side note, is the Reddit commenter who's said “semicrystalline regions are the same as secondary structure in proteins” correct ?

http://www.reddit.com/r/Biophysics/comments/1swaxs/glassy_proteins/

You can check my webside for various articles. The protein glass transition is always

induced by the solvent at the surface, it concerns only solvent coupled structural coordinates. Internal degrees of freedom like methyl group rotatation do not freeze at the glass transition.

http://www.e13.physik.tu-muenchen.de/Doster/

Thanks Dr Doster, very helpful

The classical way to detect the glass transition in protein is to monitor the temperature dependence of scattering, and this has been done by many groups.

Another approach is to measure the temperature dependence of protein functional dynamics. This latter approach was pioneered by Hans Frauenfelder (look for his articles and reviews), who did this type of studies on hemoglobin and myoglobin.

These studies produced a number of important conclusions, but I want to focus on only three:

(i) for soluble proteins their glass transition is a "slave" of the glass transition of the solvent;

(ii) the kinetic pattern of the function is changed at glass transition point from "conventional exponentials" into "distributed kinetics" mode;

(iii) although observed and studied in hemo- and myoglobin, these features should be observable in ANY protein in an appropriate temperature range.

Our group joined this field pretty late, when we found in bacteriorhodopsin (a non-soluble membrane protein) that switch from conventional exponentials to strongly non-exponential "distributed kinetics".

We published a couple of papers on this:

https://www.researchgate.net/publication/6299988_Bacteriorhodopsin_photocycle_at_cryogenic_temperatures_reveals_distributed_barriers_of_conformational_substates

https://www.researchgate.net/publication/23284898_Switch_from_conventional_to_distributed_kinetics_in_the_bacteriorhodopsin_photocycle

(have a look but first of all see the papers cited there)

Bacteriorhodopsin, being a membrane protein, undergoes the glass transition somewhat differently from that in the soluble proteins. Similar to those, the kinetic pattern of the functional dynamics chases (producing the unique "signature" of the glass transition) but this transition is not "slaved" to that of the "solvent", and the "glass transition temperature" that characterizes this switch in dynamics might be somewhat different from the temperature, which is routinely characterized by neutron scattering

Article Bacteriorhodopsin photocycle at cryogenic temperatures revea...

Article Switch from Conventional to Distributed Kinetics in the Bact...

A glassy system is generally not in thermal equilibrium, the technical term is "nonergodic". A glassy protein obtains in an MD simulation with limited duration, where some conformational degrees of freedom did not have time to relax. It is glassy because the simulation was too short. Liquids exhibit a slowest relaxation time, the alpha relaxation time, associated with the microscopic step of diffusion. For observation times longer than liquid flow relaxation, the system appears as an amorphous solid. Any system can be glassy if the observation time is short enough. The glass transition is thus defined by the crossover temperature from ergodic to nonergodic behaviour with respect to a given observation time scale. Generically, the time scale of the calorimeter, about 100 s is used: the specific heat exhibits a step at TG since slow structural degrees of freedom do not relax within 100 s below TG. The protein dynamical transition implies the freezing of structural degrees of freedom at much shorter times, 100 ps, defined by the experiment. This apparent liquid-solid transition is quite fundamental, although it is not associated with a structural change. To understand this, you dont need slaving, whatever it means, and nonexponential relaxation. A pictorial view of the glassy state involves the localisation of a single particle in a randomly chosen minimum of an energy landscape. Alternatively it is just a matter of time scales.

I agree with every word of Wolfgang, who outlined the fundamental cause of the GT. From this point of view my comment was about the "consequence": when frozen in the nonequilibrium state, the protein dynamics stops being the product of the commonly used equilibrium thermodynamics, and such "signatures" as distributed kinetics are, strickly speeking, the consequence of not the GT per se, but rather of the nonequilibrium thermodynamics, which, in turn, is a consequence of the glass transition. As a result, time and temperature are no more independent, and the faster your "scale of events and detection" the higher is the temperature where you observe the specific influence of GT on the phenomena you are studing