Abstract:
:This is the first report of its kind that well demonstrates that a lectin from Phytolacca americana [Pa-2 (P. americana lectin-2)] can also be intrinsically unordered, based on the results obtained by CD, tryptophan fluorescence, ANS (8-anilinonaphthalene-1-sulfonic acid) binding, acrylamide quenching, DLS (dynamic light scattering) and its amino acid composition database analyses. Pa-2 is an acidic monomeric lectin and acquires random coil conformation at neutral pH without any regular secondary structure. As confirmed by different spectroscopic techniques, on lowering the pH, some secondary structures, predominantly alpha-helices, are detected by far-UV CD that adopt a marginally stable partially folded collapsed conformation possessing the characteristics of a premolten globule state. It is in accordance with coil-helix transition that is commonly observed when these intrinsically unordered proteins interact with their partner molecules in vivo.
journal_name
Biosci Repjournal_title
Bioscience reportsauthors
Ahmad E,Kamranur Rahman S,Masood Khan J,Varshney A,Hasan Khan Rdoi
10.1042/BSR20090035subject
Has Abstractpub_date
2009-11-23 00:00:00pages
125-34issue
2eissn
0144-8463issn
1573-4935pii
BSR20090035journal_volume
30pub_type
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