about
Designing allostery-inspired response in mechanical networksAllosteric DNA nanoswitches for controlled release of a molecular cargo triggered by biological inputs.Phthalide Derivatives from Angelica Sinensis Decrease Hemoglobin Oxygen Affinity: A New Allosteric-Modulating Mechanism and Potential Use as 2,3-BPG Functional SubstitutesImmunological properties of oxygen-transport proteins: hemoglobin, hemocyanin and hemerythrin.Sickle Cell Hemoglobin with Mutation at αHis-50 Has Improved Solubility.Experiments on Hemoglobin in Single Crystals and Silica Gels Distinguish among Allosteric Models.Solution NMR Spectroscopy for the Study of Enzyme Allostery.Comparative Study of Elastic Network Model and Protein Contact Network for Protein Complexes: The Hemoglobin Case.Modulation of hemoglobin dynamics by an allosteric effector.Fine Sampling of the R→T Quaternary-Structure Transition of a Tetrameric Hemoglobin.Studies on the interaction between nanodiamond and human hemoglobin by surface tension measurement and spectroscopy methods.Biophysical exploration of protein-flavonol recognition: effects of molecular properties and conformational flexibility.Conformational Dynamics and Allostery in Pyruvate Kinase.New Insights into Active Site Conformation Dynamics of E. coli PNP Revealed by Combined H/D Exchange Approach and Molecular Dynamics Simulations.Tertiary and quaternary structural basis of oxygen affinity in human hemoglobin as revealed by multiscale simulations.De Novo Design of an Allosteric Metalloprotein Assembly with Strained Disulfide Bonds.Conformational Switching of a Foldamer in a Multicomponent System by pH-Filtered Selection between Competing Noncovalent Interactions.Extending the Nonbonded Cationic Dummy Model to Account for Ion-Induced Dipole Interactions.Chemical Potential of the Solvent: A Crucial Player for Rationalizing Host-Guest Affinities.Structures of the Heme Acquisition Protein HasA with Iron(III)-5,15-Diphenylporphyrin and Derivatives Thereof as an Artificial Prosthetic Group.A role of heme side-chains of human hemoglobin in its function revealed by circular dichroism and resonance Raman spectroscopy.Molecular basis of hemoglobin adaptation in the high-flying bar-headed goose.Efficiency parameters in artificial allosteric systems
P2860
Q30841681-F7DA3D23-FE36-4C30-802C-8A414CA07EA0Q33749685-F8722998-A81F-45A8-B7A1-C051F586EBB9Q33906046-CCB359C7-47B3-4808-88B5-0EC4B263EF2BQ34537178-479C6069-B61C-4305-9C48-E6A86EB9255AQ36065151-6D324E4B-8D7D-4794-BE0C-192C98702187Q36076141-5B961B20-EE20-4EC3-B82D-1689BAB99F2FQ37076848-66AFA5E7-863F-4CE0-836E-7937F83EE3C6Q37627402-F483EB9A-85BB-4CEE-A366-0ABE4A735118Q37666833-BB855C94-2201-4D63-B006-85D068F11F29Q39221168-CE6F2FC5-A5AD-4A0F-9BA6-F3C310B8A659Q39789954-68D626DC-62D8-483E-AFB4-D9DF31982E8EQ39837951-FE763955-173D-4EE4-9188-5A5DCFD5FA7BQ39995134-A83FC8A7-5453-4065-89D2-18A1676984B1Q40576779-AE19A7D9-3E01-4684-BDF3-7EFB096592ADQ41544508-443C1987-168E-4721-AD55-EB305D2D8429Q41610695-84A5F4C2-30EC-464F-942B-653B4F6D3416Q41922636-0DADB7A7-703D-41CF-8852-BB877BAD60B4Q45455183-EEEA16EA-DCBB-4D1A-B836-A8B63C356B7BQ46324299-EC856065-9ADA-410C-8F31-11CC04176416Q47663874-12AFE782-7641-48CF-8171-B610942F8BC4Q48089238-602C504B-FA02-4D06-8611-C2D9B54C0703Q55281743-5E76039F-1D4D-4DAE-ABBF-CF6497DD7E5FQ56115677-B1F6FD26-5FCB-4C8F-98D6-60C1D9A9D766
P2860
description
2015 nî lūn-bûn
@nan
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
2015年论文
@zh
2015年论文
@zh-cn
name
New look at hemoglobin allostery.
@ast
New look at hemoglobin allostery.
@en
type
label
New look at hemoglobin allostery.
@ast
New look at hemoglobin allostery.
@en
prefLabel
New look at hemoglobin allostery.
@ast
New look at hemoglobin allostery.
@en
P2093
P2860
P356
P1433
P1476
New look at hemoglobin allostery.
@en
P2093
Ming F Tam
Virgil Simplaceanu
P2860
P304
P356
10.1021/CR500495X
P50
P577
2015-01-21T00:00:00Z