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Journal article

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


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Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Inorganic Chemistry
Role:
Author
Journal:
Journal of molecular biology More from this journal
Volume:
261
Issue:
3
Pages:
443-453
Publication date:
1996-08-01
DOI:
EISSN:
1089-8638
ISSN:
0022-2836
Language:
English
Keywords:
Pubs id:
pubs:35966
UUID:
uuid:ad98fd0b-4d3c-4c6d-bafb-9e12eadd423d
Local pid:
pubs:35966
Source identifiers:
35966
Deposit date:
2012-12-19

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