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NMR spectroscopy of T4 Lysozyme peptide fragments
Authors
Najbar, L.V., Craik, D.J., Wade, J.D., McLeish, M.J.
Assembly
HELIX E
Entity
1. HELIX E (polymer, Thiol state: not present), 16 monomers, 1792.133 Da Detail

DAVRRAALIN MVFQMG


Formula weight
1792.133 Da
Exptl. method
NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 100.0 %, Completeness: 85.3 %, Completeness (bb): 93.8 % Detail

Polymer type: polypeptide(L)

Total1H
All85.3 % (81 of 95)85.3 % (81 of 95)
Backbone93.8 % (30 of 32)93.8 % (30 of 32)
Sidechain81.0 % (51 of 63)81.0 % (51 of 63)
Aromatic100.0 % (5 of 5)100.0 % (5 of 5)
Methyl90.9 % (10 of 11)90.9 % (10 of 11)

1. helix E (lys 92-107)

DAVRRAALIN MVFQMG

Sample

Temperature 288 (±0) K


#NameIsotope labelingTypeConcentration
1helix E (lys 92-107)1.0 ~ 2.0 mM
2TFE50 %
3H2O45 %
4D2O5 %

Release date
2008-11-11
Citation
Identification of initiation sites for T4 lysozyme folding using CD and NMR spectroscopy of peptide fragments
Najbar, L.V., Craik, D.J., Wade, J.D., McLeish, M.J.
Biochemistry (2000), 39, 5911-5920, PubMed 10801343 , DOI 10.1021/bi000070i ,
Related entities 1. HELIX E, : 1 : 99 : 1 : 2 entities Detail