@article { ISI:000244890900006,
	title = {Chemical, thermal and pH-induced equilibrium unfolding studies of fusarium solani lectin},
	journal = {IUBMB Life},
	volume = {59},
	number = {1},
	year = {2007},
	month = {DEC},
	pages = {34-43},
	publisher = {WILEY-BLACKWELL},
	type = {Article},
	address = {111 RIVER ST, HOBOKEN 07030-5774, NJ USA},
	abstract = {<p>The effect of urea, guanidine thiocyanate, temperature and pH was studied on the conformational stability of Fusarium solani lectin. Equilibrium unfolding with chemical denaturants showed that the lectin was least stable at pH 12 and maximally stable at pH 8.0 near its pI ( 8.7). Guanidine thiocyanate ( the concentration of denaturant at which the protein is half folded, D-1/2 = 0.49 M at pH 12) was found to be an eight times stronger denaturant than urea (D-1/2 = 3.88 M at pH 12). The unfolding curves obtained with fluorescence and CD measurements showed good agreement indicating a monophasic nature of unfolding and excluded the possibility of formation of any stable intermediate. The effect of pH on the lectin was found to be unusual as at acidic pH, the lectin showed a flexible tertiary structure with pronounced secondary structure, and retained its hemagglutinating activity. On the other hand, the lectin did not show any loss of conformation or activity upto 70 degrees C for 15 min. Moreover, thermal denaturation did not result in the aggregation or precipitation of the protein even at high temperatures. Thermal denaturation was also carried out in the presence of a low concentration of guanidine thiocyanate. Change in the enthalpy of transition (Delta H-m) varied linearly with transition temperature (T-m), which indicated that the heat capacity (Delta C-p =3.95 kJ (.) mol(-1) (.) K-1) of the lectin remained constant during the unfolding.</p>},
	keywords = {Denaturation, Fusarium solani, guanidine, Lectin, thermal, Unfolding},
	issn = {1521-6543},
	doi = {10.1080/15216540601178075},
	author = {Khan, Feroz and Ahmad, Absar and Khan, Mohammad Islam}
}
@article { ISI:000264484400007,
	title = {Comparative studies of two araceous lectins by steady state and time-resolved fluorescence and CD spectroscopy},
	journal = {Journal of Fluorescence},
	volume = {19},
	number = {2},
	year = {2009},
	month = {MAR},
	pages = {239-248},
	publisher = {SPRINGER/PLENUM PUBLISHERS},
	address = {233 SPRING ST, NEW YORK, NY 10013 USA},
	abstract = {<p>Transitions in the tryptophan microenvironment and secondary structure of two monocot lectins from Sauromatum guttatum and Arisaema tortuosum under different denaturing conditions were studied by steady state and time resolved fluorescence and CD spectroscopy. The lectins exist as tetramers with a single tryptophan residue estimated per monomer, present in a polar environment. Quenching with ionic quenchers showed predominantly electropositive environment for tryptophan residues. Acrylamide had maximum quenching effect. A decrease in KI quenching due to lectin denaturation indicated redistribution of charges as a result of possible conformational change. The two values for lifetimes of tryptophanyl population (1.2-1.4 and 6.3-6.4 ns) reduced substantially on quenching or denaturation. Similarly, both the lectins showed a drastic loss of secondary structure in 5 M Gdn-HCl or 6 M Urea or at pH 2.0 and below. For the first time araceous lectins, like legume lectins are shown to bind adenine. The presence of a compact structure at alkaline pH 10.0-12.0 was observed in CD spectra.</p>},
	keywords = {Araceae lectins, Denaturation, fluorescence, Lifetime spectroscopy, Secondary structure},
	issn = {1053-0509},
	doi = {10.1007/s10895-008-0409-z},
	author = {Dharker, Poorva N. and Gaikwad, Sushama M. and Suresh, C. G. and Dhuna, Vikram and Khan, Mohammad Islam and Singh, Jatinder and Kamboj, Sukhdev Singh}
}
