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  1. Abstract

    Variability in primary producers' responses to environmental change may buffer higher trophic levels against shifts in basal resource composition. Then again, in instances where there is a lack of functional redundancy because consumers rely on a few species to meet their energetic requirements at specific times of the year, altered community production dynamics may significantly impact food web resilience. In high‐latitude kelp forests, a complementary annual phenology of seaweed production supports coastal marine consumers' metabolic needs across large seasonal variations in their environment. Yet, marine consumers in these systems may face significant metabolic stress under the pronounced low pH conditions expected in future winters, particularly if they lack the resources to support their increased energetic demands. In this study, we investigate how the growth and nutritional value of three dominant, coexisting macroalgal species found in subpolar kelp forests will respond to ocean acidification and warming in future winter and summer seasons. We find that the three kelpsMacrocystis pyrifera,Hedophyllum nigripes, andNeoagarum fimbriatumdiffer in their vulnerability to future environmental conditions, and that the seasonal environmental context of nutrient and light availability shapes these responses. Our results suggest that poleward fringe populations ofM. pyriferamay be relatively resilient to anticipated ocean warming and acidification. In contrast, ocean warming conditions caused a decrease in the biomass and nutritional quality of both understory kelps. Considering the unique production phenology ofH. nigripes, we emphasize that negative impacts on this species in future winters may be of consequence to consumer energetics in this system. This work highlights how interspecific variation in autotrophs' responses to global change can disrupt the diversity and phenological structure of energy supply available to higher trophic levels.

     
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  2. Abstract

    The internal motions of integral membrane proteins have largely eluded comprehensive experimental characterization. Here the fast side‐chain dynamics of the α‐helical sensory rhodopsin II and the β‐barrel outer membrane protein W have been investigated in lipid bilayers and detergent micelles by solution NMR relaxation techniques. Despite their differing topologies, both proteins have a similar distribution of methyl‐bearing side‐chain motion that is largely independent of membrane mimetic. The methyl‐bearing side chains of both proteins are, on average, more dynamic in the ps–ns timescale than any soluble protein characterized to date. Accordingly, both proteins retain an extraordinary residual conformational entropy in the folded state, which provides a counterbalance to the absence of the hydrophobic effect. Furthermore, the high conformational entropy could greatly influence the thermodynamics underlying membrane‐protein functions, including ligand binding, allostery, and signaling.

     
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  3. Abstract

    The internal motions of integral membrane proteins have largely eluded comprehensive experimental characterization. Here the fast side‐chain dynamics of the α‐helical sensory rhodopsin II and the β‐barrel outer membrane protein W have been investigated in lipid bilayers and detergent micelles by solution NMR relaxation techniques. Despite their differing topologies, both proteins have a similar distribution of methyl‐bearing side‐chain motion that is largely independent of membrane mimetic. The methyl‐bearing side chains of both proteins are, on average, more dynamic in the ps–ns timescale than any soluble protein characterized to date. Accordingly, both proteins retain an extraordinary residual conformational entropy in the folded state, which provides a counterbalance to the absence of the hydrophobic effect. Furthermore, the high conformational entropy could greatly influence the thermodynamics underlying membrane‐protein functions, including ligand binding, allostery, and signaling.

     
    more » « less