Ordered water molecules as key allosteric mediators in a cooperative dimeric hemoglobin
about
A hemoglobin from plants homologous to truncated hemoglobins of microorganismsBiomolecular electrostatics and solvation: a computational perspectiveLigand migration and binding in the dimeric hemoglobin of Scapharca inaequivalvis.Structure and Ligand Selection of Hemoglobin II from Lucina pectinataLigand migration and cavities within Scapharca Dimeric HbI: studies by time-resolved crystallo-graphy, Xe binding, and computational analysisCooperative macromolecular device revealed by meta-analysis of static and time-resolved structuresTertiary and Quaternary Allostery in Tetrameric Hemoglobin from Scapharca inaequivalvisStructure of alpha-lytic protease complexed with its pro regionNon-thermal radio frequency and static magnetic fields increase rate of hemoglobin deoxygenation in a cell-free preparationA cooperative oxygen-binding hemoglobin from Mycobacterium tuberculosisStructural and dynamic properties of the homodimeric hemoglobin from Scapharca inaequivalvis Thr-72-->Ile mutant: molecular dynamics simulation, low temperature visible absorption spectroscopy, and resonance Raman spectroscopy studies.Dynamic properties of monomeric insect erythrocruorin III from Chironomus thummi-thummi: relationships between structural flexibility and functional complexity.Analysis of protein hydration in ultrahigh-resolution structures of the SRP GTPase FfhOsmotically induced helix-coil transition in poly(glutamic acid).Allosteric action in real time: time-resolved crystallographic studies of a cooperative dimeric hemoglobinStructure and dynamics of protein waters revealed by radiolysis and mass spectrometryInsight into the allosteric mechanism of Scapharca dimeric hemoglobinSynchrotron X-ray footprinting as a method to visualize water in proteins.Time-resolved x-ray crystallography of heme proteins.Suppressor mutation analysis of the sensory rhodopsin I-transducer complex: insights into the color-sensing mechanism.Electron-transfer chain in respiratory complex I.Refined atomic model of the four-layer aggregate of the tobacco mosaic virus coat protein at 2.4-A resolution.Osmotic stress, crowding, preferential hydration, and binding: A comparison of perspectives.Direct observation of cooperative protein structural dynamics of homodimeric hemoglobin from 100 ps to 10 ms with pump-probe X-ray solution scattering.Osmolyte-induced perturbations of hydrogen bonding between hydration layer waters: correlation with protein conformational changes.Allosteric hemoglobin assembly: diversity and similarity.Kinetic stability as a mechanism for protease longevity.Cooperative protein structural dynamics of homodimeric hemoglobin linked to water cluster at subunit interface revealed by time-resolved X-ray solution scattering.An optical signal correlated with the allosteric transition in Scapharca inaequivalvis HbI.Conserved waters mediate structural and functional activation of family A (rhodopsin-like) G protein-coupled receptorsCharge density-dependent modifications of hydration shell waters by Hofmeister ions.On the binding affinity of macromolecular interactions: daring to ask why proteins interact.The role of hydration on the mechanism of allosteric regulation: in situ measurements of the oxygen-linked kinetics of water binding to hemoglobin.A model for the flexibility of the distal histidine in dehaloperoxidase-hemoglobin A based on X-ray crystal structures of the carbon monoxide adduct.Allosteric effect of water in fish and human hemoglobins.Computationally accessible method for estimating free energy changes resulting from site-specific mutations of biomolecules: systematic model building and structural/hydropathic analysis of deoxy and oxy hemoglobins.Structural water as an essential comonomer in supramolecular polymerization.Distal heme pocket conformers of carbonmonoxy derivatives of Ascaris hemoglobin: evidence of conformational trapping in porous sol-gel matrices.Interfacial water effect on cooperativity and signal communication in Scapharca dimeric hemoglobin.Watching Proteins Function with Time-resolved X-ray Crystallography.
P2860
Q24555221-047800C8-2D6B-4412-B267-68B2F2A2B80CQ26853115-58EE4F31-3C38-4172-836F-95596AE00B01Q27649034-085F569E-5DC5-4905-8A22-F110400573E6Q27649553-A557D707-245C-470D-925B-9F43B36FDCABQ27658168-7C0B1AF5-1C31-43B7-909A-55FA8314F9C5Q27676225-19FEB551-E2D9-484D-85AC-0AF824B525AAQ27676689-088C7B7A-7AD5-4019-BF23-5C6D44A5F142Q27765940-7938DBCF-8C3C-4DF5-AC39-B8016E99243CQ28486156-5E44A6BE-E786-4C1F-BE3D-3563D58141A6Q28487591-03411DF8-1988-4737-BCBB-6268A78AC4BCQ28768951-B592A77E-908D-4977-972C-448D3E1E388CQ28769551-2153E498-6DED-4923-8E04-032F4FA901B7Q30358425-F45184DC-7787-4DA9-9E5E-61FB00F8246DQ30367190-7C8240A4-A057-4EDC-BE72-BB6FDBD085ACQ30477364-1E6D4A54-4D82-405E-948F-FDFF42BAC6BAQ30559588-145FBADC-6946-4A6F-80F8-2622C5C5CF19Q30865627-ACF29A8E-9BB9-4B9F-9914-98BA12169E7CQ31125696-B5A0F662-4A21-4E47-BE5A-0DA75B46FA17Q33330538-56791C04-A4BE-488C-B41F-6EC1F9EC4751Q33728571-720E8B68-562D-4DB2-9679-C718D1EB5249Q33906195-ED563EA4-C7D7-4BD6-B39D-D514B95365A3Q34167233-CF7C093F-3E6C-42B5-813D-215C36023FDCQ35667882-45CA0A52-B7DD-4636-B0E6-5EAFA55800F4Q35915623-2D58E751-07D9-40CA-8E11-95969B7C7593Q35968218-EA076D64-F9F5-4ED7-98EE-7D5C8D5139A0Q36149213-E517CFE1-5032-412D-9B81-79A6622EBFAEQ36176625-2F436F5A-F331-474C-86DE-A1202C4D480AQ36804091-65496CD7-B159-4A67-9438-7B85AF7D55CCQ36882362-CBA3F5D1-D058-455A-B8CF-0BB63EC47178Q37208884-7077EC80-1D2A-4DA9-A49E-E34F40A412E9Q37350023-FA9A46A0-9097-444B-BF34-F9F590588201Q38067023-BD469BC7-1B8B-4467-803C-9511E09A40C1Q40227545-87A28B8E-A214-488C-8705-2BF097438788Q42137143-53480A18-104D-4AD3-861A-E415093A099AQ44553724-44A73126-EFFA-4C2F-A83F-1D74770FA0BFQ44878988-1BFBE6D4-3686-46A0-BA1A-1574E35D04F7Q47144059-5B47502B-0865-4ABA-AB5A-E5E661FCD2A8Q47305676-EF528CCC-C53F-43E3-AE2F-DF745B8C6D2AQ48187925-2E497C7A-EF18-4D9A-9E5E-07C0AA15917FQ49894307-2954D071-FFA6-47C6-A7BE-0074979893B7
P2860
Ordered water molecules as key allosteric mediators in a cooperative dimeric hemoglobin
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on December 1996
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Ordered water molecules as key allosteric mediators in a cooperative dimeric hemoglobin
@en
Ordered water molecules as key allosteric mediators in a cooperative dimeric hemoglobin.
@nl
type
label
Ordered water molecules as key allosteric mediators in a cooperative dimeric hemoglobin
@en
Ordered water molecules as key allosteric mediators in a cooperative dimeric hemoglobin.
@nl
prefLabel
Ordered water molecules as key allosteric mediators in a cooperative dimeric hemoglobin
@en
Ordered water molecules as key allosteric mediators in a cooperative dimeric hemoglobin.
@nl
P2093
P2860
P356
P1476
Ordered water molecules as key allosteric mediators in a cooperative dimeric hemoglobin
@en
P2093
A Pardanani
E S Peterson
J M Friedman
Q H Gibson
P2860
P304
14526-14531
P356
10.1073/PNAS.93.25.14526
P407
P577
1996-12-01T00:00:00Z