Folding and assembly of hemoglobin monitored by electrospray mass spectrometry using an on-line dialysis system (Q80275118)

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scientific article published on 18 September 2006

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English	Folding and assembly of hemoglobin monitored by electrospray mass spectrometry using an on-line dialysis system	scientific article published on 18 September 2006

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16979901

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title

Folding and assembly of hemoglobin monitored by electrospray mass spectrometry using an on-line dialysis system (English)

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16979901

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Brian L Boys

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16979901

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Lars Konermann

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publication date

18 September 2006

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Journal of the American Society for Mass Spectrometry

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16979901

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18

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1

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8-16

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cites work

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Folding kinetics of the S100A11 protein dimer studied by time-resolved electrospray mass spectrometry and pulsed hydrogen-deuterium exchange.

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Protein structure change studied by hydrogen-deuterium exchange, functional labeling, and mass spectrometry.

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Kinetics of the reconstitution of hemoglobin from semihemoglobins alpha and beta with heme

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The kinetics of the recombination reaction between apomyoglobin and alkaline haematin

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Aggregation of deoxyhemoglobin subunits

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A global role for EKLF in definitive and primitive erythropoiesis

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The effect of the source pressure on the abundance of ions of noncovalent protein assemblies in an electrospray ionization orthogonal time-of-flight instrument

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Reconstitution of native human hemoglobin from separated globin chains and alloplex intermediates

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Spectroscopic studies of myoglobin at low pH: heme structure and ligation

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Role of alpha and beta carboxyl-terminal residues in the kinetics of human oxyhemoglobin dimer assembly

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Investigation of intact protein complexes by mass spectrometry.

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Selective oxidation of methionine beta(55)D6 at the alpha 1 beta 1 interface in hemoglobin completely destabilizes the T-state

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Coupling of folding and binding for unstructured proteins

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Dimer-monomer dissociation of human hemoglobin A.

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An abundant erythroid protein that stabilizes free alpha-haemoglobin

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Simulating disorder-order transitions in molecular recognition of unstructured proteins: where folding meets binding

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12 December 2020

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Modulation of reactivity and conformation within the T-quaternary state of human hemoglobin: the combined use of mutagenesis and sol-gel encapsulation

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Haemoglobin's chaperone

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The present view of the mechanism of protein folding

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Role of cofactors in protein folding

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Spectral demonstration of semihemoglobin formation during CN-hemin incorporation into human apohemoglobins

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Reactions of Haemoglobin Dimers after Ligand Dissociation

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Stereochemistry of Cooperative Effects in Haemoglobin: Haem–Haem Interaction and the Problem of Allostery

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Origin of the conformation dependence of protein charge-state distributions in electrospray ionization mass spectrometry

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pH changes accompanying the association of isolated alpha and beta chains of human hemoglobin

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Conformational dynamics of partially denatured myoglobin studied by time-resolved electrospray mass spectrometry with online hydrogen-deuterium exchange

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Three-dimensional Fourier Synthesis of Horse Oxyhaemoglobin at 2.8 Å Resolution: The Atomic Model

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Experimental investigation of protein folding and misfolding

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Studies of biomolecular conformations and conformational dynamics by mass spectrometry

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Is cooperative oxygen binding by hemoglobin really understood?

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Cotranslational heme binding to nascent globin chains

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The reconstitution of unfolded myoglobin with hemin dicyanide is not accelerated by fly-casting

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The kinetics of assembly of normal and variant human oxyhemoglobins.

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Electrostatic attraction governs the dimer assembly of human hemoglobin

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Expression of soluble human beta-globin chains in bacteria and assembly in vitro with alpha-globin chains.

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Ordered heme binding ensures the assembly of fully functional hemoglobin: a hypothesis

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Transfer of human alpha- to beta-hemoglobin via its chaperone protein: evidence for a new state

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NMR structure of the alpha-hemoglobin stabilizing protein: insights into conformational heterogeneity and binding

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Secondary structure of proteins through circular dichroism spectroscopy

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Consequence of beta 16 and beta 112 replacements on the kinetics of hemoglobin assembly

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Observation of the noncovalent assembly and disassembly pathways of the chaperone complex MtGimC by mass spectrometry

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Theory of protein folding

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Structure of oxidized alpha-haemoglobin bound to AHSP reveals a protective mechanism for haem

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Effects of heme addition on formation of stable human globin chains and hemoglobin subunit assembly in a cell-free system

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Molecular mechanism of AHSP-mediated stabilization of alpha-hemoglobin

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Surface and interface beta-chain residues synergistically affect hemoglobin assembly

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based on heuristic

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The kinetics and mechanism of the recombination reaction between apomyoglobin and haemin

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/16979901

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12 December 2020

based on heuristic

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Tetramer-dimer equilibrium of oxyhemoglobin mutants determined from auto-oxidation rates

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Pulsed hydrogen/deuterium exchange MS/MS for studying the relationship between noncovalent protein complexes in solution and in the gas phase after electrospray ionization

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Front-face fluorescence spectroscopy of hemoglobins

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Subunit disassembly and unfolding kinetics of hemoglobin studied by time-resolved electrospray mass spectrometry.

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Kinetics and mechanism of heme-induced refolding of human alpha-globin

1 reference

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https://pubmed.ncbi.nlm.nih.gov/16979901

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12 December 2020

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Cotranslational folding of globin

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Multiple diverse ligands binding at a single protein site: a matter of pre-existing populations

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Interface sliding as illustrated by the multiple quaternary structures of liganded hemoglobin

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based on heuristic

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Unfolding of proteins monitored by electrospray ionization mass spectrometry: a comparison of positive and negative ion modes

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Multiple equilibria of the Escherichia coli chaperonin GroES revealed by mass spectrometry

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Influence of pressure in the first pumping stage on analyte desolvation and fragmentation in nano-ESI MS.

1 reference

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based on heuristic

inferred from PubMed ID database lookup

Highly asymmetric interactions between globin chains during hemoglobin assembly revealed by electrospray ionization mass spectrometry

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12 December 2020

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Collisional cooling of large ions in electrospray mass spectrometry

1 reference

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12 December 2020

based on heuristic

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Intrinsic fluorescence of hemoglobins and myoglobins

1 reference

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12 December 2020

based on heuristic

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Quaternary Structure Regulates Hemin Dissociation from Human Hemoglobin

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based on heuristic

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Electrostatic interactions in the assembly of haemoglobin

1 reference

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https://pubmed.ncbi.nlm.nih.gov/16979901

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12 December 2020

based on heuristic

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Kinetics of deoxyhemoglobin subunit dissociation determined by haptoglobin binding: estimation of the equilibrium constant from forward and reverse rates

1 reference

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Identifiers

DOI

10.1016/J.JASMS.2006.08.013

1 reference

stated in

Europe PubMed Central

PubMed publication ID

16979901

reference URL

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:16979901%20AND%20SRC:MED&resulttype=core&format=json

retrieved

30 December 2019

Dimensions Publication ID

1052435116

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PubMed publication ID

16979901

1 reference

stated in

Europe PubMed Central

PubMed publication ID

16979901

reference URL

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:16979901%20AND%20SRC:MED&resulttype=core&format=json

retrieved

30 December 2019

 

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