About: 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

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About: 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 Goto Sponge NotDistinct Permalink

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scientific article published on 01 July 1999

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в липні 1999 (uk) article scientifique publié en 1999 (fr) artículu científicu espublizáu en xunetu de 1999 (ast) scientific article published on 01 July 1999 (en) im Juli 1999 veröffentlicher wissenschaftlicher Artikel (de)
publication date	wds:Q64004777-986AA874-1FE3-49E1-BBD8-94BE7776539B
publication date	1999-07-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q64004777-19272BA0-6442-4BFF-A4C2-D0FB070F301E
language of work or name	English
author name string	wds:Q64004777-13AD5331-14B0-4471-9458-E50239410E99 wds:Q64004777-21E7005D-3C0F-4EF5-872D-7AE306870D59 wds:Q64004777-ADB7B334-04E0-4AF8-A464-A8EB999414E7 wds:Q64004777-D2368578-6F18-4DEF-9D97-85570A89DCDC
author name string	Ho C Tsai CH Ho NT Shen TJ
rdfs:label	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 (en) 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 (nl)
skos:prefLabel	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 (en) 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 (nl)
name	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 (en) 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 (nl)
author	wds:Q64004777-234DACC5-D714-4ED6-B3D1-690E96B8E1D9
author	Chien Ho
title	wds:Q64004777-3A31B65D-C3EF-4B42-B9B2-46FCB9927828
title	Effects of substitutions of lysine and aspartic acid for asparagine at beta 108 and of tryptophan for valine at alpha 96 on the structural and functional properties of human normal adult hemoglobin: roles of alpha 1 beta 1 and alpha 1 beta 2 subunit interfaces in the cooperative oxygenation process (en)
page(s)	wds:Q64004777-573C79AF-60F1-4CA3-A71F-AB17D17BDC82
page(s)	8751-8761
instance of	wds:Q64004777-702E285A-9882-457F-BAB2-A9EB2E674C5F
instance of	scholarly article
PubMed ID	wds:Q64004777-82A4D31A-C9D5-429B-B9A1-F8BD31C1F468
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/10393550
PubMed ID	10393550
published in	wds:Q64004777-6440015D-F1DE-44C1-A34F-68AC2FC78BFF
published in	Biochemistry
issue	wds:Q64004777-BDA6B16F-0AB3-472E-9E27-9D48F3FC51CB
volume	wds:Q64004777-0EBBD224-4C0E-483B-A71D-D93DA3DB7F52
issue	27
volume	38
DOI	wds:Q64004777-63CF0122-64C5-420F-AA7D-C151975F6786
DOI	http://dx.doi.org/10.1021/BI990286O
DOI	10.1021/BI990286O
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q64004777
is cites work of	A comparative NMR study of the polypeptide backbone dynamics of hemoglobin in the deoxy and carbonmonoxy forms Introduction of a new regulatory mechanism into human hemoglobin An investigation of the distal histidyl hydrogen bonds in oxyhemoglobin: effects of temperature, pH, and inositol hexaphosphate Effector-induced structural fluctuation regulates the ligand affinity of an allosteric protein: binding of inositol hexaphosphate has distinct dynamic consequences for the T and R states of hemoglobin Single residue modification of only one dimer within the hemoglobin tetramer reveals autonomous dimer function Interfacial and distal-heme pocket mutations exhibit additive effects on the structure and function of hemoglobin Cross-linking with O-raffinose lowers oxygen affinity and stabilizes haemoglobin in a non-cooperative T-state conformation New insights into the allosteric mechanism of human hemoglobin from molecular dynamics simulations NMR investigation of the dynamics of tryptophan side-chains in hemoglobins Probing the conformation of hemoglobin presbyterian in the R-state 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 New look at hemoglobin allostery Anaerobic oxidations of myoglobin and hemoglobin by spectroelectrochemistry Expression and purification of recombinant hemoglobin in Escherichia coli A signature of the T ---> R transition in human hemoglobin A biochemical--biophysical study of hemoglobins from woolly mammoth, Asian elephant, and humans Role of β/δ101Gln in regulating the effect of temperature and allosteric effectors on oxygen affinity in woolly mammoth hemoglobin Recombinant hemoglobins with low oxygen affinity and high cooperativity WAXS studies of the structural diversity of hemoglobin in solution Deer mouse hemoglobin exhibits a lowered oxygen affinity owing to mobility of the E helix
is cites work of	wds:Q33746723-79FC8A7F-6A17-4453-A264-7BCC2A0B5E54 wds:Q34075543-75C12953-E380-4F42-82FD-44EFD2868AC9 wds:Q37624273-E9F54DCF-94BA-47A3-A6E2-D2BEB40E4FCA wds:Q44071863-C92C22CF-3486-485A-B21C-8211B405892D wds:Q44071874-4D9114D2-3AD5-48CE-BD19-57111993A4EE wds:Q64004771-D940A883-DC67-484C-A743-E5AFBEEDECFF wds:Q34178146-7C2FE64F-64C0-41D2-81E8-426C46BBAD7A wds:Q35866992-2FAE1DE6-6BFA-41F8-B942-6DB9BC907130 wds:Q74340022-B7E83AE7-A99B-48ED-9ADC-F31C0010F8EA wds:Q33916286-B02213F9-5D34-4D60-9FEB-E1640EF49A47 wds:Q37217030-FA098A56-B4C8-49C8-ACCE-2B6AC5E12962 wds:Q30400961-2363D4CD-3817-4379-9758-48DDD80DC435 wds:Q28741106-9AC22A80-BC89-45AF-8A92-330EB90A2ADE wds:Q36869693-3CDCE452-F687-4C47-86FD-04336DC0A44A wds:Q44577247-FA30E4FD-CFD7-4265-8AEA-D14845DCEDFE wds:Q33939075-F5147F1F-2896-4AFA-B7CD-FF34AC440942 wds:Q24596553-0EEACD55-7D9F-4239-9340-4BCCAD97988A wds:Q44121893-27F4B4DA-3F6E-461A-BD2F-F03C76D7D7B1 wds:Q41330941-389E9646-133C-4AA4-AB3F-FB4E893F7050 wds:Q38337951-F867F818-8AF3-4DD8-A0D8-6AB852AF905F

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