Solution structure of carbonmonoxy myoglobin determined from nuclear magnetic resonance distance and chemical shift constraints
about
Crystal structures of myoglobin-ligand complexes at near-atomic resolution.A structural basis for H-NOX signaling in Shewanella oneidensis by trapping a histidine kinase inhibitory conformationComplex of myoglobin with phenol bound in a proximal cavityNMR evidence for slow collective motions in cyanometmyoglobinUnfolding of apomyoglobin helices by synchrotron radiolysis and mass spectrometry.Protein structure determination from NMR chemical shiftsAdvances in automated NMR protein structure determination.A Study of Ion-Neutral Collision Cross Section Values for Low Charge States of Peptides, Proteins, and Peptide/Protein Complexes.Mapping molecular flexibility of proteins with site-directed spin labeling: a case study of myoglobin.Ligand binding to heme proteins. VI. Interconversion of taxonomic substates in carbonmonoxymyoglobinConnection between the taxonomic substates and protonation of histidines 64 and 97 in carbonmonoxy myoglobin.New methods of structure refinement for macromolecular structure determination by NMR.Improving the quality of NMR and crystallographic protein structures by means of a conformational database potential derived from structure databases.Conformational properties of native sperm whale apomyoglobin in solution.Structural assignment of spectra by characterization of conformational substates in bound MbCO.Chemical shifts in biomolecules.Distal residue-CO interaction in carbonmonoxy myoglobins: a molecular dynamics study of three distal mutants.Topological and sequence information predict that foldons organize a partially overlapped and hierarchical structure.Structures of protein complexes by multidimensional heteronuclear magnetic resonance spectroscopy.Molecular dynamics simulation of sperm whale myoglobin: effects of mutations and trapped CO on the structure and dynamics of cavities.On the role of thermal backbone fluctuations in myoglobin ligand gate dynamics.Enhanced conformational space sampling improves the prediction of chemical shifts in proteins.Rapid and reliable protein structure determination via chemical shift threading.The effect of heme on the conformational stability of micro-myoglobin.
P2860
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P2860
Solution structure of carbonmonoxy myoglobin determined from nuclear magnetic resonance distance and chemical shift constraints
description
1994 nî lūn-bûn
@nan
1994 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
Solution structure of carbonmo ...... and chemical shift constraints
@ast
Solution structure of carbonmo ...... and chemical shift constraints
@en
Solution structure of carbonmo ...... and chemical shift constraints
@nl
type
label
Solution structure of carbonmo ...... and chemical shift constraints
@ast
Solution structure of carbonmo ...... and chemical shift constraints
@en
Solution structure of carbonmo ...... and chemical shift constraints
@nl
prefLabel
Solution structure of carbonmo ...... and chemical shift constraints
@ast
Solution structure of carbonmo ...... and chemical shift constraints
@en
Solution structure of carbonmo ...... and chemical shift constraints
@nl
P2093
P356
P1476
Solution structure of carbonmo ...... and chemical shift constraints
@en
P2093
P304
P356
10.1006/JMBI.1994.1718
P407
P577
1994-11-25T00:00:00Z