Abstract:
:beta-Lactamase, which catalyzes beta-lactam antibiotics, is prototypical of large alpha/beta proteins with a scaffolding formed by strong noncovalent interactions. Experimentally, the enzyme is well characterized, and intermediates that are slightly less compact and having nearly the same content of secondary structure have been identified in the folding pathway. In the present study, high temperature molecular dynamics simulations have been carried out on the native enzyme in solution. Analysis of these results in terms of root mean square fluctuations in cartesian and [phi, psi] space, backbone dihedral angles and secondary structural hydrogen bonds forms the basis for an investigation of the topology of partially unfolded states of beta-lactamase. A differential stability has been observed for alpha-helices and beta-sheets upon thermal denaturation to putative unfolding intermediates. These observations contribute to an understanding of the folding/unfolding processes of beta-lactamases in particular, and other alpha/beta proteins in general.
journal_name
Biophys Jjournal_title
Biophysical journalauthors
Vijayakumar S,Vishveshwara S,Ravishanker G,Beveridge DLdoi
10.1016/S0006-3495(93)81288-8subject
Has Abstractpub_date
1993-12-01 00:00:00pages
2304-12issue
6eissn
0006-3495issn
1542-0086pii
S0006-3495(93)81288-8journal_volume
65pub_type
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