What is it about?

This study examines how different-shaped macromolecular crowders (dextran-40, ficoll-70, PEG-35) affect the unfolding of human serum albumin (HSA). Rod-shapped Dextran-40 and spherical ficoll-70 stabilize HSA while mesh PEG-35 destabilizes it mainly through entropic effects.

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Why is it important?

This study explores how different-shaped molecules affect protein behavior, mimicking crowded cell environments. It helps us understand protein stability, folding and conformotional dynamics, which is crucial for developing new drugs and treatments.

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This page is a summary of: Macromolecular crowding: how shape and interaction affect the structure, function, conformational dynamics and relative domain movement of a multi-domain protein, Physical Chemistry Chemical Physics, January 2022, Royal Society of Chemistry,
DOI: 10.1039/d1cp04842b.
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