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Chapter 18,046

Partially folded conformation of the (30-51) intermediate in the disulphide folding pathway of bovine pancreatic trypsin inhibitor. 1H and 15N resonance assignments and determination of backbone dynamics from 15N relaxation measurements

van Mierlo, C.P.; Darby, N.J.; Keeler, J.; Neuhaus, D.; Creighton, T.E.

Journal of Molecular Biology 229(4): 1125-1146

1993

ISSN/ISBN: 0022-2836
PMID: 7680380
DOI: 10.1006/jmbi.1993.1108
Accession: 018045684
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An analogue of the important folding intermediate of BPTI with only the disulphide bond between Cys30 and Cys51 has been characterized by 1H and 15N NMR techniques. In particular, the dynamics of the polypeptide backbone were characterized using (1H)-15N NOE and 15N T1 and T2 relaxation data. The intermediate is partially folded, with part of the polypeptide chain stably folded and the remainder flexible or unfolded.

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Related References

Van Mierlo, C.P.; Darby, N.J.; Creighton, T.E. 1992: The partially folded conformation of the Cys-30 Cys-51 intermediate in the disulfide folding pathway of bovine pancreatic trypsin inhibitor Proceedings of the National Academy of Sciences of the United States of America 89(15): 6775-6779
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