From computer simulations to human disease: emerging themes in protein folding

Article Abstract:

Understanding the unique functional three-dimensional structure of protein molecules is yet to be achieved by the science community. To discuss the progress of protein folding research, a three-day meeting in Madrid, Spain was organized, which 70 scientists attended. During the meeting, it was revealed that scientists are closed to solving the puzzle of protein folding, which they hope to achieve with the invention of new techniques equipment. These include stopped flow circular dichroism, protein engineering methods and stopped flow fluorescence.

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GroEL: More than just a folding cage

Article Abstract:

The chaperonin GroEL is an important but passive player in protein folding, that provides an encapsulated environment that allows folding to proceed unimpaired by aggregation. The GroEL central cavity is redesigned and it is shown that the chaperonin cage can alter the rate of folding and for some proteins, could even alter the folding mechanism.

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The crystal structure of a GroEL/peptide complex: plasticity as a basis for substrate diversity

Article Abstract:

Results show that the chaperonin GroEL in combination with cochaperonin GroES mediates protein folding in Escherichia coli. The crystal structures of the bound peptide, apical domains of GroEL, and GroEL complexes are presented.

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