Folding in the egg white
Article Abstract:
Sheena E. Radford and colleagues have made some interesting advances concerning the study of protein folding in hen egg-white lysozyme. Using pulsed hydrogen-exchange labelling and stopped-flow circular dichroism in conjunction, Radford was able to reveal complementary information that increases general knowledge of protein folding. For example, lysozyme does not fold in a kinetic two-state but rather has different rates of change in the alpha and beta domains, increasing in cooperation as the protein nears its native state.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1992
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How amino-acid insertions are allowed in an alpha-helix of T4 lysozyme
Article Abstract:
T4 lysozyme allows amino-acid insertions either by accommodation within the helix or by a looping out of its first or last turn. If the insertion is accommodated within the helix, then residues are translocated to the preceding loop. Insertions resulting in looping out within the helix are more destabilizing than those causing translocation. Which structural response follows a given insertion seems to depend on the relation between the helix and the remainder of the protein.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1993
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Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate
Article Abstract:
It has been possible to demonstrate a catalytically competent covalent glycosyl-enzyme intermediate during the catalytic cycle of hen egg-white lysozyme (HEWL). It is concluded that HEWL undertakes catalysis by the formation and subsequent breakdown of a covalent intermediate species, rather than by the formation of a long-lived ion pair.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2001
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