AbstractIn 1965 Fruchter and Crestfield (J. Biol. Chem. 240, 2868–3874) observed that dimeric RNase A prepared by lyophilization from acetic acid could be separated into two forms. Surprisingly, no other structural or functional differences could be detected between the two forms. In 1998 a structure for dimeric RNase A was determined by X-ray crystallography by Liu et al. (Proc. Natl. Acad. Sci. USA 95, 3437–3442). We found that the two forms of dimeric RNase A have indeed different structural and functional properties, and suggest that the dimer whose structure was investigated by Liu and coworkers may be identified with the lesser form of dimeric RNase A
Do the polarities of the N-terminus or the apolarity of the C-terminus of bovine RNase A influence t...
Bovine seminal RNase (BS RNase) is the only naturally dimeric member of the pancreatic-type RNase su...
RNase A oligomerizes via the three-dimensional domain-swapping mechanism to form a variety of oligom...
In 1965 Fruchter and Crestfield (J. Biol. Chem. 240, 2868-3874) observed that dimeric RNase A prepar...
Dimeric proteins can arise by the swapping of structural domains between monomers. The prevalence of...
When concentrated in mildly acidic solutions, bovine pancreatic ribonuclease (RNase A) forms long-li...
Results of gel filtration experiments performed with two different chromatographic media (Superose 1...
The thermal stability of the two dimers of RNase A with N- or C-terminal swapped ends is investigate...
When concentrated in mildly acidic solutions, bovine pancreatic ribonuclease (RNase A) forms long-li...
8 pags, 3 pagsProtein aggregation via 3D domain swapping is a complex mechanism which can lead to th...
RNase A and its minor and major dimers were digested with subtilisin under controlled conditions. Th...
Residues P19, L28, C31, and C32 have been implicated with key roles in determining the dimeric stru...
Bovine pancreatic RNase A (ribonuclease A) aggregates to form various types of catalytically active ...
By lyophilization from 40% acetic acid solutions, bovine ribonuclease A forms several types of three...
RNase A and its minor and major dimers were digested with subtilisin under controlled conditions. Th...
Do the polarities of the N-terminus or the apolarity of the C-terminus of bovine RNase A influence t...
Bovine seminal RNase (BS RNase) is the only naturally dimeric member of the pancreatic-type RNase su...
RNase A oligomerizes via the three-dimensional domain-swapping mechanism to form a variety of oligom...
In 1965 Fruchter and Crestfield (J. Biol. Chem. 240, 2868-3874) observed that dimeric RNase A prepar...
Dimeric proteins can arise by the swapping of structural domains between monomers. The prevalence of...
When concentrated in mildly acidic solutions, bovine pancreatic ribonuclease (RNase A) forms long-li...
Results of gel filtration experiments performed with two different chromatographic media (Superose 1...
The thermal stability of the two dimers of RNase A with N- or C-terminal swapped ends is investigate...
When concentrated in mildly acidic solutions, bovine pancreatic ribonuclease (RNase A) forms long-li...
8 pags, 3 pagsProtein aggregation via 3D domain swapping is a complex mechanism which can lead to th...
RNase A and its minor and major dimers were digested with subtilisin under controlled conditions. Th...
Residues P19, L28, C31, and C32 have been implicated with key roles in determining the dimeric stru...
Bovine pancreatic RNase A (ribonuclease A) aggregates to form various types of catalytically active ...
By lyophilization from 40% acetic acid solutions, bovine ribonuclease A forms several types of three...
RNase A and its minor and major dimers were digested with subtilisin under controlled conditions. Th...
Do the polarities of the N-terminus or the apolarity of the C-terminus of bovine RNase A influence t...
Bovine seminal RNase (BS RNase) is the only naturally dimeric member of the pancreatic-type RNase su...
RNase A oligomerizes via the three-dimensional domain-swapping mechanism to form a variety of oligom...