Monthly Archives: May 2017

Selectivity determinants of GPCR–G-protein binding

The selective coupling of G-protein-coupled receptors (GPCRs) to specific G proteins is critical to trigger the appropriate physiological response. However, the determinants of selective binding have remained elusive. Here we reveal the existence of a selectivity barcode (that is, patterns … Continue reading

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Intrinsically Disordered Proteins Adaptively Reorganize Cellular Matter During Stress

Intrinsically disordered proteins (IDPs) can protect cells from diverse stresses by forming higher order assemblies such as reversible aggregates or granules. Recently, Boothby et al. show that IDPs protect tardigrades against desiccation by forming a glass-like amorphous matrix, highlighting that … Continue reading

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Simultaneous quantification of protein order and disorder

Nuclear magnetic resonance spectroscopy is transforming our views of proteins by revealing how their structures and dynamics are closely intertwined to underlie their functions and interactions. Compelling representations of proteins as statistical ensembles are uncovering the presence and biological relevance … Continue reading

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The contribution of intrinsically disordered regions to protein function, cellular complexity, and human disease.

In the 1960s, Christian Anfinsen postulated that the unique three-dimensional structure of a protein is determined by its amino acid sequence. This work laid the foundation for the sequence-structure-function paradigm, which states that the sequence of a protein determines its … Continue reading

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Welcome to our sabbatical visitors!

Prof. Arthur M. Lesk from Pennsylvania State University has been visiting our group since last August, he will be here until the end of Summer. Dr Daniela Rhodes from Nanyang Technological University in Singapore visited us last month. Finally, we … Continue reading

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