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Comparative 2D NMR Studies of Human Insulin and Des-pentapeptide Insulin: Sequential Resonance Assignment and Implications for Proteins Dynamics and Receptor Recognition
Authors
Hua, Q., A, M.
Assembly
insulin B chain
Entity
1. insulin B chain (polymer), 30 monomers, 3429.919 Da Detail

FVNQHLCGSH LVEALYLVCG ERGFFYTPKT


Formula weight
3429.919 Da
Source organism
Homo sapiens
Exptl. method
NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 100.0 %, Completeness: 99.5 %, Completeness (bb): 100.0 % Detail

Polymer type: polypeptide(L)

Total1H
All99.5 % (181 of 182)99.5 % (181 of 182)
Backbone100.0 % (59 of 59)100.0 % (59 of 59)
Sidechain99.2 % (122 of 123)99.2 % (122 of 123)
Aromatic96.3 % (26 of 27)96.3 % (26 of 27)
Methyl100.0 % (17 of 17)100.0 % (17 of 17)

1. insulin B chain

FVNQHLCGSH LVEALYLVCG ERGFFYTPKT

Sample

Temperature 298 K, pH 1.9



Release date
1995-07-30
Citation
Comparative 2D NMR studies of human insulin and des-pentapeptide insulin: sequential resonance assignment and implications for protein dynamics and receptor recognition
Hua, Q., A, M.
Biochemistry (1991), 30, 5505-5515, PubMed 2036420 , DOI: ,
Related entities 1. insulin B chain, : 1 : 107 : 4 : 18 : 71 entities Detail
Interaction partners 1. insulin B chain, : 7 interactors Detail
Experiments performed 1 experiments Detail