Effect of temperature on the circular dichroism spectra of polypeptides in the extended state.
نویسندگان
چکیده
منابع مشابه
In vitro study of drug-protein interaction using electronic absorption, fluorescence, and circular dichroism spectroscopy
In the near future, design of a new generation of drugs targeting proteins will be required. Considering the complex bond between the drug and protein, the structure and stability of the target protein should be considered. So far, a series of in vitro investigations have been conducted with the aim of predicting drug-biological medium interactions. In these studies, use of spectroscopic method...
متن کاملStudying the Stability of S-Layer Protein of Lactobacillus Acidophilus ATCC 4356 in Simulated Gastrointestinal Fluids Using SDS-PAGE and Circular Dichroism
Crystalline arrays of proteinaceous subunits forming surface layers (S-layers) are now recognized as one of the most common outermost cell envelope components of prokaryotic organisms. The surface layer protein of Lactobacillus acidophilus ATCC4356 is composed of a single species of protein of apparent molecular weight of 43-46 KDa. Considering the Lactobacillus acidophilus ATCC4356 having the ...
متن کاملThe Effects of Acetaminophen on Human Serum Albumin (HSA)
Thermal conformational changes in human serum albumin (HSA) in present with a 10 mM phosphate buffer, at pH=7 have been investigated via circular dichroism (CD) and UV spectroscopic methods. The results indicate that temperature in a range of 25oC to 55oC could induce a reversible conformational change in the structure of HSA. The HSA phase transition corresponds to the physiological and patho...
متن کاملThe Effects of Acetaminophen on Human Serum Albumin (HSA)
Thermal conformational changes in human serum albumin (HSA) in present with a 10 mM phosphate buffer, at pH=7 have been investigated via circular dichroism (CD) and UV spectroscopic methods. The results indicate that temperature in a range of 25oC to 55oC could induce a reversible conformational change in the structure of HSA. The HSA phase transition corresponds to the physiological and patho...
متن کاملTheoretical studies of time-resolved spectroscopy of protein folding.
Recently, we have made significant improvements in the accuracy of calculations of the circular dichroism of proteins from first principles. The quality of these calculations (especially at 220 nm, a key wavelength, where the intensity of the band correlates well with the helical content of polypeptides) has given us confidence to use such calculations to analyse nanosecond molecular dynamics s...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- Biopolymers
دوره 11 11 شماره
صفحات -
تاریخ انتشار 1972