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Nonnative Isomers of Proline-93 and -114 Predominate in Heat-Unfolded Ribonuclease A
Authors
Adler, M., Scheraga, H.A.
Assembly
ribonuclease A
Entity
1. ribonuclease A (polymer), 124 monomers, 13690.17 Da Detail

KETAAAKFER QHMDSSTSAA SSSNYCNQMM KSRNLTKDRC KPVNTFVHES LADVQAVCSQ KNVACKNGQT NCYQSYSTMS ITDCRETGSS KYPNCAYKTT QANKHIIVAC EGNPYVPVHF DASV


Formula weight
13690.17 Da
Source organism
Bos taurus
Exptl. method
NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 8.9 %, Completeness: 4.3 %, Completeness (bb): 4.1 % Detail

Polymer type: polypeptide(L)

Total1H
All 4.3 % (31 of 714) 4.3 % (31 of 714)
Backbone 4.1 % (10 of 244) 4.1 % (10 of 244)
Sidechain 4.5 % (21 of 470) 4.5 % (21 of 470)
Aromatic 0.0 % (0 of 47) 0.0 % (0 of 47)
Methyl 4.0 % (2 of 50) 4.0 % (2 of 50)

1. ribonuclease A

KETAAAKFER QHMDSSTSAA SSSNYCNQMM KSRNLTKDRC KPVNTFVHES LADVQAVCSQ KNVACKNGQT NCYQSYSTMS ITDCRETGSS KYPNCAYKTT QANKHIIVAC EGNPYVPVHF DASV

Sample

Temperature 323 K, pH 2



Release date
1995-07-30
Citation
Nonnative isomers of proline-93 and -114 predominate in heat-unfolded ribonuclease A
Adler, M., Scheraga, H.A.
Biochemistry (1990), 29, 8211-8216, PubMed 2252883 , DOI 10.1021/bi00488a003 ,
Related entities 1. ribonuclease A, : 1 : 101 : 94 entities Detail
Interaction partners 1. ribonuclease A, : 8 interactors Detail