About: Site mutations disrupt inter-helical H-bonds (α14W–α67T and β15W–β72S) involved in kinetic steps in the hemoglobin R→T transition without altering the free energies of oxygenation

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About: Site mutations disrupt inter-helical H-bonds (α14W–α67T and β15W–β72S) involved in kinetic steps in the hemoglobin R→T transition without altering the free energies of oxygenation Goto Sponge NotDistinct Permalink

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scientific article published on 01 January 2003

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rdf:type	Item
description	wetenschappelijk artikel (nl) 2003 թվականին հրատարակված գիտական հոդված (hy) наукова стаття, опублікована в грудні 2002 (uk) article scientifique publié en 2003 (fr) im Jahr 2003 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu en xineru de 2003 (ast) artikull shkencor i botuar më 01 janar 2003 (sq) scientific article published on 01 January 2003 (en)
publication date	wds:Q64004771-DE83FDA4-B7C2-4544-9703-377211A15B0F
publication date	2003-01-01 00:00:00Z (xsd:dateTime)
cites work	wds:Q64004771-081A8F7F-D482-4CDD-8577-85CEE8C00FD6 wds:Q64004771-141C1EDD-91B3-4A69-B6D9-52ED09278049 wds:Q64004771-148CE433-1560-42A5-9350-EB592FF3F880 wds:Q64004771-1D610597-A1A2-4731-992D-E76DE8FACDBD wds:Q64004771-1D677174-2B24-4A10-A0D0-335047D974A4 wds:Q64004771-25FDA6D8-A508-4F59-A464-BF23CCD397D4 wds:Q64004771-52E86DA0-540F-4059-B595-0818AE0F3FA1 wds:Q64004771-5927AAEC-1591-4932-878F-FB9C566B8AC0 wds:Q64004771-5A92346F-70E5-4F42-854A-6BDB24DBC29D wds:Q64004771-612455E2-212C-4DBA-9CCD-42FC45CB86B5 wds:Q64004771-6750B495-BF77-4837-BF62-9B468730AC77 wds:Q64004771-67E10A92-9C92-4962-91C6-398304DEEA8C wds:Q64004771-6B42A21C-274E-4584-A89B-6F5E4D96A10F wds:Q64004771-7CC71C32-1C25-44E1-BF34-F9763B2E8333 wds:Q64004771-7D3A59C2-3E0D-4D55-A593-966B726FFF21 wds:Q64004771-7F4016D7-ED4D-499B-81F8-2B049E2A6CBE wds:Q64004771-8033F129-4790-4783-9786-044D51E0FE64 wds:Q64004771-82C30555-1E1F-4D03-B1FD-571B4225A454 wds:Q64004771-869D3338-6648-4BD7-9E1E-67B60F4E5682 wds:Q64004771-A0AAB811-4038-4169-BEE6-3E828A1A8278 wds:Q64004771-A155E419-9804-4328-8208-C35AEC3F7CD1 wds:Q64004771-A71EDE36-7F7F-41B0-AE8B-F59783AB272F wds:Q64004771-BA658335-85EC-48BA-88FA-6B38130D1396 wds:Q64004771-D37D2F53-E83A-4945-9FDD-E2EA5ABB5693 wds:Q64004771-D940A883-DC67-484C-A743-E5AFBEEDECFF wds:Q64004771-E7BC9036-5B81-4E9E-9C59-E73F909CB843 wds:Q64004771-E8BE4C64-D540-4109-8868-0D0596982182 wds:Q64004771-E99A023A-638B-4CB2-8624-C64E1EAE8C91 wds:Q64004771-EB74F6C8-10CA-4582-8F41-D84261878510 wds:Q64004771-EF5E19C9-2378-497A-8A72-CD2081FF9212 wds:Q64004771-F18E3633-8802-4DC2-8E6D-3855006830A5 wds:Q64004771-F5536E31-D905-4F94-9796-9A1B1ABBDFDF wds:Q64004771-F8FECBD7-FE32-4D5D-B4EA-541ECB7D9A41 wds:Q64004771-F9F6CF3C-E017-401A-9EB6-8B2AF0A69D26
cites work	Structure of human oxyhaemoglobin at 2.1 A resolution Stereochemistry of Cooperative Effects in Haemoglobin: Haem–Haem Interaction and the Problem of Allostery A TROSY CPMG sequence for characterizing chemical exchange in large proteins A proton nuclear Overhauser effect investigation of the subunit interfaces in human normal adult hemoglobin Proton nuclear magnetic resonance studies on hemoglobin: cooperative interactions and partially ligated intermediates Chain-selective isotopic labeling for NMR studies of large multimeric proteins: application to hemoglobin Restoring allosterism with compensatory mutations in hemoglobin NMR reveals hydrogen bonds between oxygen and distal histidines in oxyhemoglobin Effects of amino acid substitutions at beta 131 on the structure and properties of hemoglobin: evidence for communication between alpha 1 beta 1- and alpha 1 beta 2-subunit interfaces Effects of Substitutions of Lysine and Aspartic Acid for Asparagine at β108 and of Tryptophan for Valine at α96 on the Structural and Functional Properties of Human Normal Adult Hemoglobin: Roles of α1β1and α1β2Subunit Interfaces in the Coopera A Novel Low Oxygen Affinity Recombinant Hemoglobin (α96Val→Trp): Switching Quaternary Structure Without Changing the Ligation State Proton nuclear Overhauser effect investigation of the heme pockets in ligated hemoglobin: conformational differences between oxy and carbonmonoxy forms Nuclear magnetic resonance studies of hemoglobins. VII. Tertiary structure around ligand binding site in carbonmonoxyhemoglobin The crystal structure of human deoxyhaemoglobin at 1.74 A resolution An enzymic reduction system for metmyoglobin and methemoglobin, and its application to functional studies of oxygen carriers Production of unmodified human adult hemoglobin in Escherichia coli Production of human normal adult and fetal hemoglobins in Escherichia coli Proton nuclear magnetic resonance investigation of structural changes associated with cooperative oxygenation of human adult hemoglobin NMR investigation of the dynamics of tryptophan side-chains in hemoglobins A test of the role of the proximal histidines in the Perutz model for cooperativity in haemoglobin NMR study of the phosphoryl binding loop in purine nucleotide proteins: evidence for strong hydrogen bonding in human N-ras p21. Contribution of surface histidyl residues in the alpha-chain to the Bohr effect of human normal adult hemoglobin: roles of global electrostatic effects. The structure of human carbonmonoxy haemoglobin at 2.7 A resolution Proton nuclear magnetic resonance study of the quaternary structure of human hemoglobins in water Site-directed mutagenesis in hemoglobin: functional and structural role of inter- and intrasubunit hydrogen bonds as studied with 37 beta and 145 beta mutations Hemoglobin allostery: resonance Raman spectroscopy of kinetic intermediates New light on allostery: dynamic resonance Raman spectroscopy of hemoglobin kempsey. Nanosecond dynamics of the R-->T transition in hemoglobin: ultraviolet Raman studies An Additional H-Bond in the α1β2Interface as the Structural Basis for the Low Oxygen Affinity and High Cooperativity of a Novel Recombinant Hemoglobin (βL105W)† UV resonance raman spectra of ligand binding intermediates of sol-gel encapsulated hemoglobin Extension of transverse relaxation-optimized spectroscopy techniques to allosteric proteins: CO- and paramagnetic fluoromet-hemoglobin [beta (15N-valine)] Contributions of asparagine at alpha 97 to the cooperative oxygenation process of hemoglobin Roles of alpha 114 and beta 87 amino acid residues in the polymerization of hemoglobin S: implications for gene therapy Role of Interhelical H-Bonds (Wα14−Tα67 and Wβ15−Sβ72) in the Hemoglobin Allosteric Reaction Path Evaluated by UV Resonance Raman Spectroscopy of Site-Mutants
author name string	wds:Q64004771-04F8EED5-81C3-4DF7-9245-73C67766F13A wds:Q64004771-0FBA39AC-C751-4BD1-B0D2-A52BB2523CF7 wds:Q64004771-3CAFE266-25B2-4327-9894-69D672DED083 wds:Q64004771-46935F17-5516-4D9A-A837-429CE6B3E07B wds:Q64004771-93ADEB2E-BD46-4ADE-8836-5CEC7EDC82C0 wds:Q64004771-AE1200F6-634D-491E-84AE-3AF9FE762418 wds:Q64004771-EC17E74E-1991-486D-9545-D15343CE05B8
author name string	Thomas G Spiro Chien Ho Nancy T Ho Virgil Simplaceanu Tong-Jian Shen Ching-Hsuan Tsai Daojing Wang
rdfs:label	Site mutations disrupt inter-helical H-bonds (α14W–α67T and β15W–β72S) involved in kinetic steps in the hemoglobin R→T transition without altering the free energies of oxygenation (en) Site mutations disrupt inter-helical H-bonds (α14W–α67T and β15W–β72S) involved in kinetic steps in the hemoglobin R→T transition without altering the free energies of oxygenation (sq) Site mutations disrupt inter-helical H-bonds (nl)
skos:prefLabel	Site mutations disrupt inter-helical H-bonds (α14W–α67T and β15W–β72S) involved in kinetic steps in the hemoglobin R→T transition without altering the free energies of oxygenation (en) Site mutations disrupt inter-helical H-bonds (α14W–α67T and β15W–β72S) involved in kinetic steps in the hemoglobin R→T transition without altering the free energies of oxygenation (sq) Site mutations disrupt inter-helical H-bonds (nl)
name	Site mutations disrupt inter-helical H-bonds (α14W–α67T and β15W–β72S) involved in kinetic steps in the hemoglobin R→T transition without altering the free energies of oxygenation (en)

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