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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., Weiss, M.A.
Assembly
insulin A chain
Entity
1. insulin A chain (polymer), 21 monomers, 2383.696 Da Detail

GIVEQCCTSI CSLYQLENYC N


Formula weight
2383.696 Da
Source organism
Homo sapiens
Exptl. method
NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 100.0 %, Completeness: 99.2 %, Completeness (bb): 100.0 % Detail

Polymer type: polypeptide(L)

Total1H
All99.2 % (119 of 120)99.2 % (119 of 120)
Backbone100.0 % (42 of 42)100.0 % (42 of 42)
Sidechain98.7 % (77 of 78)98.7 % (77 of 78)
Aromatic100.0 % (8 of 8)100.0 % (8 of 8)
Methyl100.0 % (11 of 11)100.0 % (11 of 11)

1. insulin A chain

GIVEQCCTSI CSLYQLENYC N

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., Weiss, M.A.
Biochemistry (1991), 30, 5505-5515, PubMed 2036420 , DOI 10.1021/bi00236a025 ,
Related entities 1. insulin A chain, : 1 : 110 : 9 : 7 : 74 entities Detail
Interaction partners 1. insulin A chain, : 2 interactors Detail
Experiments performed 1 experiments Detail