Persistence of native-like topology in a denatured protein in 8 M urea.
Experimental methods have demonstrated that when a protein unfolds, not all of its structure is lost. Here we report measurement of residual dipolar couplings in denatured forms of the small protein staphylococcal nuclease oriented in strained polyacrylamide gels. A highly significant correlation among the dipolar couplings for individual residues suggests that a native-like spatial positioning and orientation of chain segments (topology) persists to concentrations of at least 8 molar urea. These data demonstrate that long-range ordering can occur well before a folding protein attains a compact conformation, a conclusion not anticipated by any of the standard models of protein folding.
Shortle
D
D
Department of Biological Chemistry, The Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA. shortle@welchlink.welch.jhu.edu
Ackerman
M S
MS
D000180:Acrylic Resins; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D008836:Micrococcal Nuclease / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D014508:Urea
D000180:Acrylic Resins; C016680:polyacrylamide gels; D014508:Urea; D008836:Micrococcal Nuclease