Add to ORKGThe unfolding of proteins during denaturation by guanidine or urea has been extensively studied. However, the methods hitherto employed usually provide only a limited amount of information on gross changes of such molecular properties as shape, size, or the exposure of buried aromatic residues. ...03249-25
AbstractDynamic light scattering and circular dichroism experiments were performed to determine the ...
We undertook a detailed comparative analysis of the infrared spectra of wild-type ribonuclease T1 an...
The pressure stability of ribonuclease A under native and reducing conditions was investigated with ...
To address a number of conflicting reports in the literature, we undertook an infrared spectroscopic...
We undertook a first detailed comparative analysis of the refolding kinetics of ribonuclease A (RNas...
ABSTRACT: Guanidinium (Gdm+) is a widely used denaturant, but it is still largely unknown how it ope...
Fourier transform-infrared (FT-IR) spectra are reported for the amide III spectral region of the nat...
The secondary structure of ribonuclease T1 (RNase T1) in aqueous solution and its temperature-induce...
Although many salts denature proteins (e.g. guanidine hydrochloride and guanidine thiocyanate) or st...
AbstractTwo mechanisms have been proposed for the thermal unfolding of ribonuclease S (RNase S). The...
The secondary structure of ribonuclease T1 (RNase T1) in aqueous solution and its temperature-induce...
We introduce near-IR spectroscopy as an ancillary tool for monitoring structural changes of proteins...
Near-infrared fluorescent proteins (NIR FPs) based on the complexes of bacterial phytochromes with t...
The denatured states of proteins have always attracted our attention due to the fact that the denatu...
AbstractThe denaturation of dimeric creatine kinase (CK) induced by urea and guanidine hydrochloride...
AbstractDynamic light scattering and circular dichroism experiments were performed to determine the ...
We undertook a detailed comparative analysis of the infrared spectra of wild-type ribonuclease T1 an...
The pressure stability of ribonuclease A under native and reducing conditions was investigated with ...
To address a number of conflicting reports in the literature, we undertook an infrared spectroscopic...
We undertook a first detailed comparative analysis of the refolding kinetics of ribonuclease A (RNas...
ABSTRACT: Guanidinium (Gdm+) is a widely used denaturant, but it is still largely unknown how it ope...
Fourier transform-infrared (FT-IR) spectra are reported for the amide III spectral region of the nat...
The secondary structure of ribonuclease T1 (RNase T1) in aqueous solution and its temperature-induce...
Although many salts denature proteins (e.g. guanidine hydrochloride and guanidine thiocyanate) or st...
AbstractTwo mechanisms have been proposed for the thermal unfolding of ribonuclease S (RNase S). The...
The secondary structure of ribonuclease T1 (RNase T1) in aqueous solution and its temperature-induce...
We introduce near-IR spectroscopy as an ancillary tool for monitoring structural changes of proteins...
Near-infrared fluorescent proteins (NIR FPs) based on the complexes of bacterial phytochromes with t...
The denatured states of proteins have always attracted our attention due to the fact that the denatu...
AbstractThe denaturation of dimeric creatine kinase (CK) induced by urea and guanidine hydrochloride...
AbstractDynamic light scattering and circular dichroism experiments were performed to determine the ...
We undertook a detailed comparative analysis of the infrared spectra of wild-type ribonuclease T1 an...
The pressure stability of ribonuclease A under native and reducing conditions was investigated with ...