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N.m.r. study of conformational changes in lysozyme around the thermal transition point
Authors
Bernard, M., Canioni, P., Cozzone, P., Berthou, J., Jolles, P.
Assembly
lysozyme
Entity
1. lysozyme (polymer), 129 monomers, 14297.99 Da Detail

KVFGRCELAA AMKRHGLDNY RGYSLGNWVC AAKFESNFNT QATNRNTDGS TDYGILQINS RWWCNDGRTP GSRNLCNIPC SALLSSDITA SVNCALKIVS DGNGMNAWVA WRNRCKGTDV QAWIRGCRL


Formula weight
14297.99 Da
Source organism
Gallus gallus
Exptl. method
NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 10.1 %, Completeness: 3.1 %, Completeness (bb): 0.5 % Detail

Polymer type: polypeptide(L)

Total13C
All 3.1 % (17 of 548) 3.1 % (17 of 548)
Backbone 0.5 % (2 of 375) 0.5 % (2 of 375)
Sidechain 5.9 % (17 of 290) 5.9 % (17 of 290)
Aromatic 0.0 % (0 of 59) 0.0 % (0 of 59)
Methyl24.6 % (15 of 61)24.6 % (15 of 61)

1. lysozyme

KVFGRCELAA AMKRHGLDNY RGYSLGNWVC AAKFESNFNT QATNRNTDGS TDYGILQINS RWWCNDGRTP GSRNLCNIPC SALLSSDITA SVNCALKIVS DGNGMNAWVA WRNRCKGTDV QAWIRGCRL

Sample

Temperature 311 K, pH 4.76



Release date
1995-07-30
Citation
N.m.r. study of conformational changes in lysozyme around the thermal transition point
Bernard, M., Canioni, P., Cozzone, P., Berthou, J., Jolles, P.
Int. J. Pept. Protein Res. (1986), 27, 643-652, PubMed 3759336 ,
Related entities 1. lysozyme, : 1 : 103 : 99 entities Detail
Interaction partners 1. lysozyme, : 8 interactors Detail