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Effect of the single mutation His 64->Phe on the stability and folding of apomyoglobin
Authors
Garcia, C., Cavagnero, S., Nishimura, C., Dyson, H.JANE., Wright, P.E.
Assembly
myoglobin H64F mutant
Entity
1. myoglobin (polymer, Thiol state: not present), 153 monomers, 17209.69 Da Detail

VLSEGEWQLV LHVWAKVEAD VAGHGQDILI RLFKSHPETL EKFDRFKHLK TEAEMKASED LKKFGVTVLT ALGAILKKKG HHEAELKPLA QSHATKHKIP IKYLEFISEA IIHVLHSRHP GDFGADAQGA MNKALELFRK DIAAKYKELG YQG


Formula weight
17209.69 Da
Source organism
Physeter catodon
Exptl. method
NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 100.0 %, Completeness: 39.2 %, Completeness (bb): 67.9 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All39.2 % (722 of 1842)25.0 % (239 of 956)46.2 % (335 of 725)91.9 % (148 of 161)
Backbone67.9 % (610 of 899)52.3 % (158 of 302)67.9 % (304 of 448)99.3 % (148 of 149)
Sidechain23.3 % (253 of 1085)12.7 % (83 of 654)40.6 % (170 of 419) 0.0 % (0 of 12)
Aromatic 1.2 % (2 of 162) 2.5 % (2 of 81) 0.0 % (0 of 79) 0.0 % (0 of 2)
Methyl29.3 % (54 of 184)21.7 % (20 of 92)37.0 % (34 of 92)

1. myoglobin

VLSEGEWQLV LHVWAKVEAD VAGHGQDILI RLFKSHPETL EKFDRFKHLK TEAEMKASED LKKFGVTVLT ALGAILKKKG HHEAELKPLA QSHATKHKIP IKYLEFISEA IIHVLHSRHP GDFGADAQGA MNKALELFRK DIAAKYKELG YQG

Sample

Temperature 308 (±0.5) K, pH 5.8 (±0.2)


#NameIsotope labelingTypeConcentration
1myoglobin[U-95% 13C; U-90% 15N]1 mM

Release date
2000-03-22
Citation
Changes in the apomyoglobin folding pathway caused by mutation of the distal histidine residue
Garcia, C., Nishimura, C., Cavagnero, S., Dyson, H.JANE., Wright, P.E.
Biochemistry (2000), 39, 11227-11237, PubMed 10985768 , DOI 10.1021/bi0010266 ,
Related entities 1. myoglobin, : 1 : 2 : 93 : 106 entities Detail
Interaction partners 1. myoglobin, : 2 interactors Detail
Experiments performed 2 experiments Detail
Keywords apomyoglobin folding, folding intermediate, molten globule, mutant