Add to ORKGMethods for macromolecular structure determination (NMR and crystallography) are now being used to get structural information on partially folded and unfolded states of proteins. These techniques, in combination with proton hydrogen exchange studies are powerful tools to extract information on non-native states of proteins. This review discusses progress In this area of protein folding
The second edition of Structure in Protein Chemistry showcases the latest developments and innovatio...
ABSTRACT All possible protein folding intermediates exist in equilibrium with the na-tive protein at...
How the information content of an unfolded polypeptide sequence directs a protein towards a well-for...
Methods for macromolecular structure determination (NMR and crystallography) are now being used to g...
Deciphering the mechanism of protein folding is one of the most desirable goals in the field of stru...
Recent progress has advanced our abilities to use NMR spectroscopy to follow - in real time - the st...
AbstractNMR spectroscopy is a powerful tool for the investigation of protein folding and misfolding,...
Proteins in nature have evolved to perform specific functions. The functional properties of proteins...
Advances in hardware, sample preparation, pulse sequence development and refinement techniques have ...
Pioneering work in the 1980s has established NMR spectroscopy as a routine method for protein struct...
This thesis describes an investigation of the folding and stability of a series of derivatives of th...
Understanding the forces involved in protein folding is necessary for the development of reliable mo...
protein folding intermediates Exchange rates of individual amide protons in the polypeptide backbone...
grantor: University of TorontoThe isolated N-terminal SH3 domain of the Drosophila signali...
Protein folding is a reaction in which an extended polypeptide chain acquires maximal packing throug...
The second edition of Structure in Protein Chemistry showcases the latest developments and innovatio...
ABSTRACT All possible protein folding intermediates exist in equilibrium with the na-tive protein at...
How the information content of an unfolded polypeptide sequence directs a protein towards a well-for...
Methods for macromolecular structure determination (NMR and crystallography) are now being used to g...
Deciphering the mechanism of protein folding is one of the most desirable goals in the field of stru...
Recent progress has advanced our abilities to use NMR spectroscopy to follow - in real time - the st...
AbstractNMR spectroscopy is a powerful tool for the investigation of protein folding and misfolding,...
Proteins in nature have evolved to perform specific functions. The functional properties of proteins...
Advances in hardware, sample preparation, pulse sequence development and refinement techniques have ...
Pioneering work in the 1980s has established NMR spectroscopy as a routine method for protein struct...
This thesis describes an investigation of the folding and stability of a series of derivatives of th...
Understanding the forces involved in protein folding is necessary for the development of reliable mo...
protein folding intermediates Exchange rates of individual amide protons in the polypeptide backbone...
grantor: University of TorontoThe isolated N-terminal SH3 domain of the Drosophila signali...
Protein folding is a reaction in which an extended polypeptide chain acquires maximal packing throug...
The second edition of Structure in Protein Chemistry showcases the latest developments and innovatio...
ABSTRACT All possible protein folding intermediates exist in equilibrium with the na-tive protein at...
How the information content of an unfolded polypeptide sequence directs a protein towards a well-for...