Familiar strangers
Article Abstract:
Recent research has reported more examples of three previously observed protein folds. The structure of the amino-terminal domain of the staphylococcal enterotoxin B has been observed in staphylococcal nuclease and two other proteins. The structure of Src-homology domain of spectrin is similar to that of R67 dihydrofolate reductase. Lastly, hisactophilin has the beta-trefoil fold common to interleukin-1 and fibroblast growth factors. The similarity of fold types in the presence of sequence dissimilarity suggests that a few folds perform a great number of functions.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1992
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Further up the kinetic pathway
Article Abstract:
A pathway of cooperative interaction may exist side-by-side with the protein-folding pathway. Moreover, a chaperone protein, GroEL, may assist in transferring protein from the partially folded to the fully folded state. Thomas Langer and colleagues have produced evidence confirming that proteins refold in vitro along a different pathway. The newly discovered pathway may be the body's means of guarding the proteins from interference as they carry out their functions within the cells.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1992
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Direct NMR evidence for an intermediate preceding the rate-limiting step in the unfolding of ribonuclease A
Article Abstract:
The mechanism of the unfolding of ribonuclease A involves one unfolding intermediate. In the rate-limiting step, the side chains of the intermediate freely rotate at a critical degree of expansion of the protein. This intermediate is an expression of dry molten globule. During the protein unfolding, instead of a damage in the side chain interactions, the hydrogen bond network is collapsed as a rate-limiting event.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1995
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