In:
FEBS Letters, Wiley, Vol. 438, No. 1-2 ( 1998-10-30), p. 127-130
Abstract:
Protein S, a two‐domain spore coat protein from Myxococcus xanthus , is structurally related to eye‐lens βγ‐crystallins. No natural monomeric one‐domain member of this protein superfamily is known. To determine the stability of the single domains and to explain the ubiquitous domain duplication, the isolated domains of protein S were constructed. The N‐domain is thermodynamically more stable than the C‐domain. In intact protein S, domain interactions lead to an apparent decrease in stability of the N‐terminal domain, whereas the C‐terminal domain is stabilised. In contrast, unfolding kinetics of both domains are decreased 100‐fold due to interactions in the complete molecule.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1016/S0014-5793(98)01287-3
Language:
English
Publisher:
Wiley
Publication Date:
1998
detail.hit.zdb_id:
1460391-3
SSG:
12
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