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Weiergraeber, O. H.

Publications and source records attributed to Weiergraeber, O. H..

2 recordsLinked to original sources

The molecular origin of body temperature in homeothermic species

We propose the Interfacial Water Quantum-transition model (IWQ model) explaining temperature-dependent functional transitions in proteins. The model postulates that measured critical temperatures, TC, correspond to reference temperatures, TW, defined by rotational quantum transitions of temporarily free water molecules at the protein-water interface. The models applicability is demonstrated through transitions in hemoglobin and thermosensitive TRP channels. We suggest this mechanism also defines basal body temperatures in homeotherms, with TW=36.32{degrees}C for humans. We demonstrate that human (mammal) and chicken (Aves) body temperatures align with specific reference temperatures, and correlate with pronounced transitions at TC in hemoglobin oxygen saturation. This suggests evolutionary adaptations in homeotherms involve an interplay between oxygen supply and waters rotational transition temperatures. The IWQ-model states that proteins sense and water sets critical physiological temperatures. Significance StatementWe propose the Interfacial Water Quantum-transition (IWQ) model that offers a new way to understand how proteins respond to critical temperature changes. We suggest that the key temperatures at which proteins change their function are linked to specific quantum transitions of water molecules at the protein-water interface. This model explains why certain critical temperatures, like human body temperature, align with these transitions. By exploring this connection in proteins like hemoglobin and in thermosensitive channels, the IWQ model highlights a fundamental link between water behavior and biological temperature regulation, shedding light on evolutionary adaptations in humans and other animals.

biophysics↗

Highlighting the hidden: A tagging strategy for monitoring the association of GABARAP with microtubules in living cells

GABARAP, like other ATG8 proteins, is a ubiquitin-like modifier and its C-terminal lipid conjugation enables association with cellular membranes. To prevent interference with the lipidation process, N-terminal fluorescent protein (FP) tagging strategies have become the standard for studying ATG8 localization and function in living cells, significantly contributing to our understanding of this protein familys multifaceted roles. However, recent findings have unveiled potential limitations of bulky N-terminal tags, particularly regarding ATG8 functionality and localization in specific contexts. This study employed live cell imaging with particular emphasis on the GABARAP split-tandem construct, GABARAP(G116A)-mTagBFP2-GABARAP (G-B-G), which retains both a free N-terminus and a lipidation-competent C-terminus. Notably, our results revealed a robust association of G-B-G with the microtubule network in living cells which was not observed with N-terminal FP fusions of GABARAP, although early in vitro studies demonstrated an interaction of GABARAP and tubulin. Since we observed alteration of the microtubule network organization for G-B-G, this construct emerges as a valuable tool, which can help shedding light on potential roles of GABARAP in microtubule-associated processes that are integral to autophagy-related and -unrelated cellular transport.

cell biology↗