Very high resolution structure of a trematode hemoglobin displaying a TyrB10-TyrE7 heme distal residue pair and high oxygen affinity
about
A TyrCD1/TrpG8 hydrogen bond network and a TyrB10TyrCD1 covalent link shape the heme distal site of Mycobacterium tuberculosis hemoglobin O.The hemoglobins of the trematodesFasciola hepaticaandParamphistomum epiclitum: A molecular biological, physico-chemical, kinetic, and vaccination studyMolecular characterization of Clonorchis sinensis secretory myoglobin: delineating its role in anti-oxidative survival.Thr-E11 regulates O2 affinity in Cerebratulus lacteus mini-hemoglobin.Peroxidase activity and involvement in the oxidative stress response of roseobacter denitrificans truncated hemoglobin.Refinement by shifting secondary structure elements improves sequence alignments.O2 migration pathways are not conserved across proteins of a similar fold.Rapid comparison of properties on protein surfaceConservation of the three-dimensional structure in non-homologous or unrelated proteins.A globin domain in a neuronal transmembrane receptor of Caenorhabditis elegans and Ascaris suum: molecular modeling and functional properties.Molecular dynamics free energy calculations to assess the possibility of water existence in protein nonpolar cavitiesKinetic modulation in carbonmonoxy derivatives of truncated hemoglobins: the role of distal heme pocket residues and extended apolar tunnel.Functional implications of the proximal site hydrogen bonding network in Vitreoscilla hemoglobin (VHb): role of Tyr95 (G5) and Tyr126 (H12).Multiple active site conformers in the carbon monoxide complexes of trematode hemoglobins.Clues for discovering a new biological function of Vitreoscilla hemoglobin in organisms: potential sulfide receptor and storage.
P2860
Q27641095-EB27536C-0F8F-4ECF-A9C5-6B1CE37F468FQ27651178-0BA0D0B1-D11F-49AC-88A0-39F8FFB83955Q33756092-0F71832E-FAD2-4B2B-A365-D8CA2483ADCEQ34322860-514AE576-5F5A-4894-B8B0-712BD82F213CQ35556614-A5838F63-B7FF-41AA-B6A5-90F36912FCA3Q35848801-09E8305F-0B1D-4210-933C-45CC42FC5825Q36129090-3BC08C1D-9AF7-4B66-9D5A-6D939AA48CE2Q36952014-48C795DA-A998-4ED8-9483-553E99751F01Q38067794-DB9B293D-363C-4D5D-A35A-CF063B0B03C3Q39715813-FA187A03-2B0A-4FC6-82EE-2A44F6522326Q41006570-0804FEEF-4C0B-46D8-860C-9C91E2C0894EQ44433301-2450DAB1-5320-4AE4-8B5E-4032DB25FD5BQ46356775-AE150757-ACC1-4887-AD48-8439ED8AA4CFQ46947012-FB38614D-3108-4F57-8BCE-2BFCDE4F81C7Q51434753-741779D8-C237-4720-A8D2-582B84E0963A
P2860
Very high resolution structure of a trematode hemoglobin displaying a TyrB10-TyrE7 heme distal residue pair and high oxygen affinity
description
2001 nî lūn-bûn
@nan
2001 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Very high resolution structure ...... pair and high oxygen affinity
@ast
Very high resolution structure ...... pair and high oxygen affinity
@en
Very high resolution structure ...... pair and high oxygen affinity
@nl
type
label
Very high resolution structure ...... pair and high oxygen affinity
@ast
Very high resolution structure ...... pair and high oxygen affinity
@en
Very high resolution structure ...... pair and high oxygen affinity
@nl
prefLabel
Very high resolution structure ...... pair and high oxygen affinity
@ast
Very high resolution structure ...... pair and high oxygen affinity
@en
Very high resolution structure ...... pair and high oxygen affinity
@nl
P2093
P356
P1476
Very high resolution structure ...... pair and high oxygen affinity
@en
P2093
J Vanfleteren
M C Marden
M L Van Hauwaert
P304
P356
10.1006/JMBI.2001.4731
P407
P577
2001-06-22T00:00:00Z