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Disulfide crosslinks to probe the structure and flexibility of a designed four-helix bundle protein
Lynne Regan,
Arlene Rockwell,
Zelda Wasserman,
William Degrado,
Lynne Regan
The Experimental Station, E.I. du Pont de Nemours and Company, Wilmington, Delaware 19880
Search for more papers by this authorArlene Rockwell
The Experimental Station, E.I. du Pont de Nemours and Company, Wilmington, Delaware 19880
Search for more papers by this authorZelda Wasserman
The Experimental Station, E.I. du Pont de Nemours and Company, Wilmington, Delaware 19880
Search for more papers by this authorWilliam Degrado
The Experimental Station, E.I. du Pont de Nemours and Company, Wilmington, Delaware 19880
Search for more papers by this authorLynne Regan,
Arlene Rockwell,
Zelda Wasserman,
William Degrado,
Lynne Regan
The Experimental Station, E.I. du Pont de Nemours and Company, Wilmington, Delaware 19880
Search for more papers by this authorArlene Rockwell
The Experimental Station, E.I. du Pont de Nemours and Company, Wilmington, Delaware 19880
Search for more papers by this authorZelda Wasserman
The Experimental Station, E.I. du Pont de Nemours and Company, Wilmington, Delaware 19880
Search for more papers by this authorWilliam Degrado
The Experimental Station, E.I. du Pont de Nemours and Company, Wilmington, Delaware 19880
Search for more papers by this authorAbstract
The introduction of disulfide crosslinks is a generally useful method by which to identify regions of a protein that are close together in space. Here we describe the use of disulfide crosslinks to investigate the structure and flexibility of a family of designed 4-helix bundle proteins. The results of these analyses lend support to our working model of the proteins' structure and suggest that the proteins have limited main-chain flexibility.
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