Collin opened discussion of Tomas Polivka ’ s paper: It would be very interesting to study the excited state dynamics of this E-FCP protein in the context of the whole organism. Dynamics and behavior are frequently altered in an in vivo sample compared to an isolated one. As an example, I ’ d like to present some recent results from Graham Fleming ’ s group at UC Berkeley in which we apply in vivo spectroscopy to study the photoprotective quenching mechanisms in intact cells of the heterokont algae Nannochloropsis oceanica . 1 N. oceanica is a small marine algae, 2 – 3 m M in size, which results in minimized light scattering compared to larger organisms such as E. huxleyi . It also possesses a relatively simple membrane structure and pigment composition including the higher plant xanthophyll cycle carotenoids (violaxanthin-antheraxanthin-zeaxanthin), one type of chlorophyll, and Chl a -binding LHCX proteins, which are closely related to the FCP proteins discussed in the present contribution (DOI: 10.1039/ c8fd00193f). We have also made use of two knock-out mutants of N. oceanica : vde , which is unable to synthesize Zea in high light, and lhcx1 , which lacks the LHCX1 the conformations of single-stranded thymine due to the over-stabilisation of 5 0 -thymine in a syn conformation. 1 Do you observe similar e ff ects in – 1258. Spiridoula Matsika responded: The study by McCamant focused on single stranded thymine strands and dinucleotides, and it was concluded that the current AMBER force eld does not accurately predict the conformation of single-stranded thymine. Our work considers double stranded oligonucleotides which is expected to be much better represented by AMBER force elds. That said, we do not have a direct way to compare our results to experiments to verify the validity of the simulations. Our results, however, indirectly agree with experiment, and we believe
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Ashfold et al. (2019) studied this question.