About this Research Topic
Complex organization in both human societies and living cells relies on communication between their elements. Indeed, most cellular functions arise when communication is established through biomolecules that physically and specifically contact each other in a concerted manner to transmit messages efficiently.
‘Molecular sociology’ within cells involves binding events between macromolecules, such as protein–protein, protein–nucleic acid, protein–carbohydrate and protein–membrane interactions, that are acutely orchestrated to sustain the life–death balance. These interactions between biomolecules occur on a wide range of timescales. Stable complexes, with lifetimes ranging from minutes to days, involve high affinity and high specificity binding. Amongst many others, these include irreversible enzyme inhibition and the assembly of proteins supporting the cell’s ultrastructure. Weak complexes are characterized by a fine balance between specificity of binding and fast turnover rate, with the majority displaying equilibrium dissociation constants within the micromolar or even millimolar range. Perhaps counter-intuitively, these weaker molecular recognition mechanisms are not uncommon and play key roles in many biological processes, including electron transfer chains in respiration and photosynthesis and the cell signalling cascades involving kinases and phosphatases.
Due to technical limitations, weak complexes remain poorly understood despite their critical role in many biological events inside the cell. Over the last few years, specific tools have been developed to analyse more transient intermolecular interactions, including NMR paramagnetic relaxation enhancement and kinetic approaches. These methods have recently been complemented by high-throughput techniques to identify novel biomolecules that wealy bind to each other. Such advances make the analysis of the transient biointeractome (the so-called trans-biointeractome) more affordable. Overall, trans-biointeractome analysis remains highly dependent on the specific technique employed. Therefore, the study of weakly interacting systems can be reliably tackled in depth only by an integrative and holistic approach combining in vitro strategies with other methods to detect such interactions within the cell. Hence, we invite submissions of manuscripts that measure, analyze or review weak interactions within or between any cellular machinery e.g. ribosomal or proteasomal interactions, electron transfer reactions, phosphorylation cascades, cytoskeletal contacts and many more.
‘Molecular sociology’ within cells involves binding events between macromolecules, such as protein–protein, protein–nucleic acid, protein–carbohydrate and protein–membrane interactions, that are acutely orchestrated to sustain the life–death balance. These interactions between biomolecules occur on a wide range of timescales. Stable complexes, with lifetimes ranging from minutes to days, involve high affinity and high specificity binding. Amongst many others, these include irreversible enzyme inhibition and the assembly of proteins supporting the cell’s ultrastructure. Weak complexes are characterized by a fine balance between specificity of binding and fast turnover rate, with the majority displaying equilibrium dissociation constants within the micromolar or even millimolar range. Perhaps counter-intuitively, these weaker molecular recognition mechanisms are not uncommon and play key roles in many biological processes, including electron transfer chains in respiration and photosynthesis and the cell signalling cascades involving kinases and phosphatases.
Due to technical limitations, weak complexes remain poorly understood despite their critical role in many biological events inside the cell. Over the last few years, specific tools have been developed to analyse more transient intermolecular interactions, including NMR paramagnetic relaxation enhancement and kinetic approaches. These methods have recently been complemented by high-throughput techniques to identify novel biomolecules that wealy bind to each other. Such advances make the analysis of the transient biointeractome (the so-called trans-biointeractome) more affordable. Overall, trans-biointeractome analysis remains highly dependent on the specific technique employed. Therefore, the study of weakly interacting systems can be reliably tackled in depth only by an integrative and holistic approach combining in vitro strategies with other methods to detect such interactions within the cell. Hence, we invite submissions of manuscripts that measure, analyze or review weak interactions within or between any cellular machinery e.g. ribosomal or proteasomal interactions, electron transfer reactions, phosphorylation cascades, cytoskeletal contacts and many more.
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