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Characterization of the Structure and Dynamics of Amyloidogenic Variants of Human Lysozyme by NMR Spectroscopy
Authors
Chamberlain, A.K., Receveur, V., Spencer, A., Redfield, C., Dobson, C.M.
Assembly
Human Lysozyme
Entity
1. Human Lysozyme (polymer, Thiol state: not reported), 130 monomers, 14700.53 Da Detail

KVFERCELAR TLKRLGMDGY RGISLANWMC LAKWESGYNT RATNYNAGDR STDYGIFQIN SRYWCNDGKT PGAVNACHLS CSALLQDNIA DAVACAKRVV RDPQGIRAWV AWRNRCQNRD VRQYVQGCGV


Formula weight
14700.53 Da
Source organism
Homo sapiens
Exptl. method
NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 94.6 %, Completeness: 28.4 %, Completeness (bb): 61.9 % Detail

Polymer type: polypeptide(L)

Total1H15N
All28.4 % (265 of 934)18.3 % (141 of 771)76.1 % (124 of 163)
Backbone61.9 % (239 of 386)45.0 % (116 of 258)96.1 % (123 of 128)
Sidechain 4.7 % (26 of 548) 4.9 % (25 of 513) 2.9 % (1 of 35)
Aromatic 0.0 % (0 of 71) 0.0 % (0 of 66) 0.0 % (0 of 5)
Methyl 6.3 % (4 of 63) 6.3 % (4 of 63)

1. lysozyme

KVFERCELAR TLKRLGMDGY RGISLANWMC LAKWESGYNT RATNYNAGDR STDYGIFQIN SRYWCNDGKT PGAVNACHLS CSALLQDNIA DAVACAKRVV RDPQGIRAWV AWRNRCQNRD VRQYVQGCGV

Sample

Temperature 310 (±1) K, pH 5.0 (±0.2)


#NameIsotope labelingTypeConcentration
1lysozyme0.8 ~ 1.2 mM
2HCl0.0 ~ 0.0 mM
3H2O100 %

Release date
2002-01-24
Citation
Characterization of the structure and dynamics of amyloidogenic variants of human lysozyme by NMR spectroscopy
Chamberlain, A.K., Receveur, V., Spencer, A., Redfield, C., Dobson, C.M.
Protein Sci. (2001), 10, 2525-2530, PubMed 11714920 , DOI 10.1110/ps.28101 ,
Related entities 1. Human Lysozyme, : 1 : 34 : 43 : 25 : 100 entities Detail
Interaction partners 1. Human Lysozyme, : 43 interactors Detail
Experiments performed 3 experiments Detail
Keywords amyloid fibrils, backbone dynamics, lysozyme, mutant, NMR