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Conformational and Dynamic Characterization of the Molten Globule state of an Apomyoglobin Mutant with an altered Folding Pathway
Authors
Cavagnero, S., Nishimura, C., Schwarzinger, S., Dyson, J., Wright, P.E.
Assembly
apomyoglobin N132G,E136G mutant
Entity
1. apomyoglobin N132G,E136G mutant (polymer, Thiol state: not present), 153 monomers, 17070.54 Da Detail

VLSEGEWQLV LHVWAKVEAD VAGHGQDILI RLFKSHPETL EKFDRFKHLK TEAEMKASED LKKHGVTVLT ALGAILKKKG HHEAELKPLA QSHATKHKIP IKYLEFISEA IIHVLHSRHP GDFGADAQGA MGKALGLFRK DIAAKYKELG YQG


Formula weight
17070.54 Da
Source organism
Physeter catodon
Exptl. method
NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 97.4 %, Completeness: 32.7 %, Completeness (bb): 63.1 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All32.7 % (597 of 1826)16.7 % (158 of 947)41.9 % (301 of 719)86.3 % (138 of 160)
Backbone63.1 % (566 of 897)44.0 % (133 of 302)66.1 % (295 of 446)92.6 % (138 of 149)
Sidechain 3.6 % (39 of 1069) 3.9 % (25 of 645) 3.4 % (14 of 413) 0.0 % (0 of 11)
Aromatic 0.0 % (0 of 156) 0.0 % (0 of 78) 0.0 % (0 of 76) 0.0 % (0 of 2)
Methyl 4.3 % (8 of 184) 4.3 % (4 of 92) 4.3 % (4 of 92)

1. apomyoglobin

VLSEGEWQLV LHVWAKVEAD VAGHGQDILI RLFKSHPETL EKFDRFKHLK TEAEMKASED LKKHGVTVLT ALGAILKKKG HHEAELKPLA QSHATKHKIP IKYLEFISEA IIHVLHSRHP GDFGADAQGA MGKALGLFRK DIAAKYKELG YQG

Sample

Temperature 323 (±1) K, pH 4.1 (±0.1)


#NameIsotope labelingTypeConcentration
1apomyoglobin[U-13C; U-15N]0.3 mM
2ethanol[U-2H]10 %
3H2O90 %

Release date
2002-01-24
Citation
Conformational and dynamic characterization of the molten globule state of an apomyoglobin mutant with an altered folding pathway
Cavagnero, S., Nishimura, C., Schwarzinger, S., Dyson, H.JANE., Wright, P.E.
Biochemistry (2001), 40, 14459-14467, PubMed 11724558 , DOI 10.1021/bi011500n ,
Related entities 1. apomyoglobin N132G,E136G mutant, : 1 : 93 : 108 entities Detail
Interaction partners 1. apomyoglobin N132G,E136G mutant, : 2 interactors Detail
Experiments performed 6 experiments Detail