study the interaction of ni complex of tetradentate schiff base ligand with hen egg white lysozyme
نویسندگان
چکیده
abstractinteraction of ni complex(salen= n, n´-ethylene bis(salicylideneimine)) with hen egg-white lysozyme (hewl) was studied by absorption spectroscopy, competitive binding study and thermal denaturation study. the protein binding affinity of ni complex was found to be (3.0×103m−1). the binding plot obtained from the absorption titration data gives a binding constant of 2.4 (± 0.3)×103 m-1. it was found that the charge transfer band of the metal complex was perturbed in the presence of (hewl). thermal denaturation study of hewl with ni complex revealed the δtm of 5±0.2 °c. the thermodynamic parameters (δhº > 0 and δsº > 0) showed that the hydrophobic interaction leads to the increasing entropy which is brought about by interaction with the complex. the negative δgº values for interaction of hewl with the ni complex indicate the spontaneity of the complexation.
منابع مشابه
Study the Interaction of Ni Complex of Tetradentate Schiff Base Ligand with HEN Egg White Lysozyme
AbstractInteraction of Ni complex(Salen= N, N´-ethylene bis(salicylideneimine)) with hen egg-white lysozyme (HEWL) was studied by absorption spectroscopy, competitive binding study and thermal denaturation study. The protein binding affinity of Ni complex was found to be (3.0×103M−1). The binding plot obtained from the absorption titration data gives a binding constant of 2.4 (± 0.3)×103 M...
متن کاملHen Egg - white Lysozyme Crystals
Proton tautomerism is a general phenomenon in organic molecules and plays a vital role in many fields of chemistry and biochemistry. The tautomerism of salicylideneanilines [eq(1)] has attracted a considerable attention because it is closely related to thermoand photochromism. Salicylideneanilines greatly favor the enol form over the cis-keto form in the gas phase. We demonstrate here that the ...
متن کاملCharacterization of the unfolding pathway of hen egg white lysozyme.
After the recent discovery of a ribonuclease A unfolding intermediate [Kiefhaber, T., et al. (1995) Nature 375, 513-515], we investigated the unfolding pathway of hen egg white lysozyme. At pH* 4.00 with D2O at 10 degrees C and 6 M guanidinium chloride, unfolding shows a single, slow kinetic phase, with a relaxation time of 3300 s when monitored by circular dichroism (CD). Exchange of the trypt...
متن کاملIR and Raman spectroscopic studies of the interaction of trehalose with hen egg white lysozyme.
Infrared and Fourier transform Raman spectra are reported for dried mixtures of trehalose and lysozyme. The Raman spectra show effects on the protein amide I band and some sugar bands that are not present when the components are dried separately. Comparison of ir spectra with those published previously show significant differences. It is concluded that these arise because of differences in the ...
متن کاملRefinement of triclinic hen egg-white lysozyme at atomic resolution.
X-ray diffraction data have been collected at both low (120 K) and room temperature from triclinic crystals of hen egg-white lysozyme to 0.925 and 0.950 A resolution, respectively, using synchrotron radiation. Data from one crystal were sufficient for the low-temperature study, whereas three crystals were required at room temperature. Refinement was carried out using the programs PROLSQ, ARP an...
متن کاملHigh-pressure protein crystallography of hen egg-white lysozyme
Crystal structures of hen egg-white lysozyme (HEWL) determined under pressures ranging from ambient pressure to 950 MPa are presented. From 0.1 to 710 MPa, the molecular and internal cavity volumes are monotonically compressed. However, from 710 to 890 MPa the internal cavity volume remains almost constant. Moreover, as the pressure increases to 950 MPa, the tetragonal crystal of HEWL undergoes...
متن کاملمنابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
physical chemistry researchجلد ۵، شماره ۱، صفحات ۱۱۳-۱۲۳
کلمات کلیدی
میزبانی شده توسط پلتفرم ابری doprax.com
copyright © 2015-2023