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Folding Funnels Key to Biomimicry

By Guest PostNovember 9, 2012Scienceafm, archaea, array, atomic force microscopy, babak sanii, bacteria, berkeley lab, biomimicry, biomolecular nanomachines, bones, carolyn bertozzi, cell, collagen matrices, collagen monomers, concept, fabrication, folding funnel, free energy, function, humans, jim deyoreo, key, kinetic traps, luis comolli, mica surface, molecular foundry, molecule level, molecules, multiple proteins, nanoscale synthesis, Nature, ordered structure, organic scaffolds, properties, protein folding, protein structure, proteins, pseudohexagonal symmetry, s layer, self assemble, seong ho shin, sungwook chung, surface layer, teeth

Berkeley Lab Finding that Protein Folding Funnels Also Apply to Self-Assembly Should Benefit Biomimicry and Nanosynthesis

Proteins are able to self-assemble into a wide range of highly ordered structures that feature a diverse array of properties. Through biomimicry – technological innovation inspired by nature – humans hope to emulate proteins and produce our own version of self-assembling molecules. A key to accomplishing this is understanding how protein-folding – a process critical to the form and function of a protein – is extended from individual proteins to complex assemblies.

Researchers with the U.S. Department of Energy (DOE)’s Lawrence Berkeley National Laboratory (Berkeley Lab) have now shown that a concept widely accepted as describing the folding of a single individual protein is also applicable to the self-assembly of multiple proteins. Their findings provide important guidelines for future biomimicry efforts, particularly for device fabrication and nanoscale synthesis. (more…)

Correct Protein Folding:

*Berkeley Lab Researchers Identify Structure of Key Control Element Behind Protein Misfolding That Can Lead to Disease*

The gold standard for nanotechnology is nature’s own proteins. These biomolecular nanomachines – macromolecules forged from peptide chains of amino acids – are able to fold themselves into a dazzling multitude of shapes and forms that enable them to carry out an equally dazzling multitude of functions fundamental to life. As important as protein folding is to virtually all biological systems, the mechanisms behind this process have remained a mystery. The fog, however, is being lifted.

A team of researchers with the U.S. Department of Energy (DOE)’s Lawrence Berkeley National Laboratory (Berkeley Lab), using the exceptionally bright and powerful x-ray beams of the Advanced Light Source, have determined the crystal structure of a critical control element within chaperonin, the protein complex responsible for the correct folding of other proteins. The incorrect or “misfolding” of proteins has been linked to many diseases, including Alzheimer’s, Parkinson’s and some forms of cancer. (more…)

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Folding Funnels Key to Biomimicry

Correct Protein Folding: