Reading, writing and redesigning
Article Abstract:
Lynne Regan and colleagues have been able to redesign a protein into a completely different fold by exchanging only 50% of its amino acids. Their work, undertaken in response to a challenge issued by George Rose and Trevor Creamer in 1994, was based around converting the B1 domain of protein G into a new protein. This protein had the folded structure of repressor of primer (Rop), another protein. The researchers were able to build an appropriate core structure based on their existing characterization of simplified core variants of Rop.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1997
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Folding with a two-stroke motor
Article Abstract:
Considerable progress has been made in the understanding of the power of crystallography, and in particular the interaction between the molecular chaperone GroEL and CroES, which is necessary for some proteins to fold. Three dimensional electron-microscopic image reconstructions showed that as well as the binding of ATP and GRoES, there is an upward movement of the GroEL apical domains. There are suggestions that GroEL can unfold misfolded proteins, so that they reach the native state.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1997
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Trapped in the act
Article Abstract:
A model protein bearing a peptide tag that targets it for degradation is globally unfolded by a member of the Clp/Hsp100 protein family known as ClpA. It is possible for ClpA to change the conformation of a substrate protein, unfolding it and then transmitting it directly to ClpP. It is likely that global unfolding is a general feature while a substrate protein translocates from ClpA into the proteolytic chamber of ClpP.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1999
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