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Insight into a random coil conformation and an isolated helix: structural and dynamical characterisation of the C-helix peptide from hen lysozyme.

Abstract:

A 17 residue peptide corresponding to the C-helix of hen lysozyme (residues 86 to 102) has been investigated in detail to assess the factors that determine its conformation in both aqueous and trifluoroethanol (TFE) solutions. A thorough characterisation of the peptide by CD and NMR techniques under both conditions has been performed including the determination of complete NMR proton sequential assignments, and measurement of NOE effects, 3JHN alpha coupling constants, temperature coefficient...

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Publication status:
Published

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Publisher copy:
10.1006/jmbi.1996.0475

Authors


Pitkeathly, M More by this author
Miranker, A More by this author
More by this author
Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Inorganic Chemistry
Dobson, CM More by this author
Journal:
Journal of molecular biology
Volume:
261
Issue:
3
Pages:
443-453
Publication date:
1996-08-05
DOI:
EISSN:
1089-8638
ISSN:
0022-2836
URN:
uuid:ad98fd0b-4d3c-4c6d-bafb-9e12eadd423d
Source identifiers:
35966
Local pid:
pubs:35966

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