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FRAGMENT 33-61 OF BOVINE alpha-HEMOGLBIN: THE EFFECT OF C-TERMINAL AMIDATION AND IDENTIFICATION OF THE MINIMAL PORTION WITH ANTIFUNGAL ACTIVITY
Authors
Machado, A., Sforca, M.L., Miranda, A., Daffre, S., Spisni, A., Pertinhez, T.A., Miranda, M.M.
Assembly
amidated fragment 48-61 of bovine alpha-hemoglobin
Entity
1. amidated fragment 48-61 of bovine alpha-hemoglobin (polymer, Thiol state: not present), 15 monomers, 1374.527 Da Detail

LSHGSAQVKG HGAKX


Formula weight
1374.527 Da
Source organism
Bos taurus
Exptl. method
NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 93.3 %, Completeness: 73.3 %, Completeness (bb): 87.1 % Detail

Polymer type: polypeptide(L)

Total1H
All73.3 % (55 of 75)73.3 % (55 of 75)
Backbone87.1 % (27 of 31)87.1 % (27 of 31)
Sidechain63.6 % (28 of 44)63.6 % (28 of 44)
Aromatic 0.0 % (0 of 4) 0.0 % (0 of 4)
Methyl50.0 % (3 of 6)50.0 % (3 of 6)

1. amidated fragment 48-61

LSHGSAQVKG HGAKX

Sample

Temperature 310 (±1) K


#NameIsotope labelingTypeConcentration
1amidated fragment 48-610.0 ~ 1.0 mM

Release date
2008-07-15
Citation 1
The micelle-bound structure of an antimicrobial peptide derived from the alpha-chain of bovine hemoglobin isolated from the tick Boophilus microplus
Sforca, M.L., Machado, A., Figueredo, R.C., Oyama, S., Silva, F.D., Miranda, A., Daffre, S., Miranda, M.TERESA., Spisni, A., Pertinhez, T.A.
Biochemistry (2005), 44, 6440-6451, PubMed 15850378 , DOI 10.1021/bi0475323 ,
Citation 2
NMRPipe: a multidimensional spectral processing system based on UNIX pipes
Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J., Bax, A.
J. Biomol. NMR (1995), 6, 277-293, PubMed 8520220 ,
Related entities 1. amidated fragment 48-61 of bovine alpha-hemoglobin, : 1 : 141 : 60 entities Detail
Interaction partners 1. amidated fragment 48-61 of bovine alpha-hemoglobin, : 32 interactors Detail
Experiments performed 4 experiments Detail
Chemical shift validation 3 contents Detail
Keywords antimicrobial peptide, MINIMAL PEPTIDE SEQUENCE, STRUCTURAL REQUIREMENTS