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Local interactions drive the formation of non-native structure in the denatured state of human alpha-lactalbumin: A high resolution structural characterization of a peptide model in aqueous solution
Authors
Demarest, S.J., Hua, Y., Raleigh, D.P.
Assembly
LCA
Entity
1. LCA (polymer, Thiol state: not present), 13 monomers, 1324.549 Da Detail

XIDYWLAHKA LAX


Formula weight
1324.549 Da
Source organism
Homo sapiens
Exptl. method
NMR
Refine. method
DISTANCE GEOMETRY AND SIMULATED ANNEALING
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 84.6 %, Completeness: 100.0 %, Completeness (bb): 100.0 % Detail

Polymer type: polypeptide(L)

Total1H
All100.0 % (68 of 68)100.0 % (68 of 68)
Backbone100.0 % (22 of 22)100.0 % (22 of 22)
Sidechain100.0 % (46 of 46)100.0 % (46 of 46)
Aromatic100.0 % (12 of 12)100.0 % (12 of 12)
Methyl100.0 % (9 of 9)100.0 % (9 of 9)

1. LCA

XIDYWLAHKA LAX

Sample

Pressure 1 atm, Temperature 283 K, pH 2.8


#NameIsotope labelingTypeConcentration
1LCA0.0 ~ 0.0 mM

Protein Blocks Logo
Calculated from 40 models in PDB: 1CB3, Strand ID: A Detail


Release date
2015-04-14
Citation
Local interactions drive the formation of nonnative structure in the denatured state of human alpha-lactalbumin: a high resolution structural characterization of a peptide model in aqueous solution
Demarest, S.J., Hua, Y., Raleigh, D.P.
Biochemistry (1999), 38, 7380-7387, PubMed 10353850 , DOI 10.1021/bi990320z ,
Related entities 1. LCA, : 1 : 1 entities Detail
Experiments performed 4 experiments Detail
nullKeywords alpha-lactalbumin, molten globule state, non-native interactions, protein folding