I came across it when looking for a paper on structural analysis of a protein (for a biochem subject) with the condition that it was co-authored by someone at UQ. Initially I looked at the first name from UQ which was Sean C. Smith and thought no idea who that is but who cares it fits the criteria. It wasn't untill today that I thought hey maybe that paper would have something interesting to talk about for biophys and had a second look at it. To my surprise the paper actually had two people listed as from UQ the second of which was "SETH OLSEN"! I'm not sure how I managed to miss that the first time.
The paper talks about both chromophores (organic molecules which can provide some of those vivid colours we see in plants and animals) and fluorescent proteins, both of which have a very similar structure with only a small conformational change providing their functional diversity.
The paper is:
The 2.1 A° Crystal Structure of the Far-red Fluorescent Protein HcRed: Inherent Conformational Flexibility of the Chromophore, J. Mol. Biol. (2005) 349, pg. 223–237.
Here is the abstract and I accessed the paper through the UQ library site.
Am I above flattery? A good question...
ReplyDeleteI have been working on the cis-trans photoisomerization of these molecules since I was a scientific gamete. I still am.
I think that this sort of behavior is probably widespread in FPs. There is evidence for this, but this was one of the first examples where a trans noncoplanar conformation was specifically tied to a non-emitting population in the resting protein. Others have emerged since then. There is data going back to the mid-nineties which in retrospect suggests that most FPs have dark populations. I believe that isomerism of the chromophore is a good explanation, but really there may be something deeper going on... isomerism may be a symptom of a fundamentally electronic change in the chromohore chemistry. Luckily, this change would be easy to explain in class, because it can be summarized with a few simple Lewis structures.