Abstract：
:By means of 2D NMR techniques, all backbone resonances in the 1H NMR spectrum of the single-stranded DNA binding protein encoded by gene V of the filamentous phage IKe have been assigned sequence specifically (at pH 4.6, T = 298 K). In addition, a major part of the side chain resonances could be assigned as well. Analysis of NOESY data permitted the elucidation of the secondary structure of IKe gene V protein. The major part of this secondary structure is present as an antiparallel beta-sheet, i.e., as two beta-loops which partly combine into a triple-stranded beta-sheet structure, one beta-loop and one triple-stranded beta-sheet structure. It is shown that a high degree of homology exists with the secondary structure of the single-stranded DNA binding protein encoded by gene V of the distantly related filamentous phage M13.
journal_name
Biochemistryjournal_title
Biochemistryauthors
van Duynhoven JP,Folkers PJ,Prinse CW,Harmsen BJ,Konings RN,Hilbers CWdoi
10.1021/bi00119a039subject
Has Abstractpub_date
1992-02-04 00:00:00pages
1254-62issue
4eissn
0006-2960issn
1520-4995journal_volume
31pub_type
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