Disulfide crosslinks to probe the structure and flexibility of a designed four-helix bundle protein.
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.
Regan
L
L
Experimental Station, E.I. du Pont de Nemours and Company, Wilmington, Delaware 19880, USA.
Rockwell
A
A
Wasserman
Z
Z
DeGrado
W
W
D000595:Amino Acid Sequence; D002850:Chromatography, Gel; D002942:Circular Dichroism; D003198:Computer Simulation; D003553:Cystine / Q000737:chemistry*; D018257:Helix-Loop-Helix Motifs; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009038:Motion; D010084:Oxidation-Reduction; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry; D011487:Protein Conformation; D011489:Protein Denaturation; D015202:Protein Engineering; D017433:Protein Structure, Secondary
D010455:Peptides; D003553:Cystine