Protein flexibility acclimatizes photosynthetic energy conversion to the ambient temperature
Article Abstract:
A meticulous adjustment of energy conversion rate, resulting in similar yields from mesophiles and thermophiles is described. The novel biochemical mechanism has provided new guidelines for manipulating the acclimatization of enzymes to the ambient temperatures of diverse habitats and has revealed novel protein elements that are important for modulating structure-activity relationships in membrane and globular proteins alike.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2006
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Natural-like function in artificial WW domains
Article Abstract:
Artificial WW sequences function like their natural counterparts, showing class-specific recognition of proline-containing target peptides are demonstrated. The ability to recapitulate natural-like function in designed sequences shows that a relatively small quantity of sequence information is sufficient to specify the global energetics of amino acid interactions.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2005
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Evolutionary information for specifying protein fold
Article Abstract:
The sequence rules for specifying a protein fold by computationally creating artificial protein sequences are defined, using only statistical information encoded in a multiple sequence alignment. The relative simplicity of the information used for creating sequences suggests a marked reduction to the potential complexity of the protein-folding problem.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2005
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