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The extremely slow alpha-helix/beta-sheet transition of proteins is a crucial step in amylogenic diseases and represents an internal rearrangement of local contacts in an already folded protein. These internal structural rearrangements within an already folded protein are a critical aspect of biological action and are a product of conformational flow along unknown metastable local minima of the energy landscape of the compact protein. We use a diffusional IR mixer with time-resolved Fourier transform IR spectroscopy capable of 400-micros time resolution to show that the trifluoroethanol driven beta-sheet to alpha-helix transition of beta-lactoglobulin proceeds via a compact beta-sheet intermediate with a lifetime of 7 ms, small compared with the overall folding time of beta-lactoglobulin.
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N C Darnton, and
R H Austin, and
C Batt, and
K Gerwert
May 2005,
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E Kauffmann, and
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K Gerwert
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K Gerwert
June 2001,
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K Gerwert
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Proteins,
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C Batt, and
K Gerwert
March 1982,
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E Kauffmann, and
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