Increase in apparent compressibility of cytochrome c upon oxidation.
about
Evidence of protein collective motions on the picosecond timescaleUse of metal oxide nanoparticle band gap to develop a predictive paradigm for oxidative stress and acute pulmonary inflammationDecomposition of protein experimental compressibility into intrinsic and hydration shell contributions.Resilience of the iron environment in heme proteins.Adiabatic compressibility of globular proteinsProtein compressibility, dynamics, and pressure.The redox couple of the cytochrome c cyanide complex: the contribution of heme iron ligation to the structural stability, chemical reactivity, and physiological behavior of horse cytochrome c.Calculation of volume fluctuation for globular protein modelsDynamics of heme iron in crystals of metmyoglobin and deoxymyoglobinCategorization of lipophilic xenobiotics by the enthalpic structure-function response of hepatic mixed-function oxidase.The effect of high pressure upon proteins and other biomolecules.Adiabatic compressibility of myosin subfragment-1 and heavy meromyosin with or without nucleotide.Coupled motion in proteins revealed by pressure perturbationStructural analysis of diheme cytochrome c by hydrogen-deuterium exchange mass spectrometry and homology modelingReduction of thioredoxin significantly decreases its partial specific volume and adiabatic compressibility.The cytochrome c fold can be attained from a compact apo state by occupancy of a nascent heme binding site.Effects of Corneal Hydration on Brillouin Microscopy In Vivo.Large oxidation dependence observed in terahertz dielectric response for cytochrome cForce to Unbind Ligand-Receptor Complexes and the Internal Rigidity of Globular Proteins Probed by Single-Molecule Force Spectroscopy
P2860
Q28386166-48F29B89-6BED-4509-96CB-3A05ADCCC7B1Q28392757-5CE9FAED-9ABE-41AB-B29B-FDFB2A488708Q30478855-63C2DBB7-0236-4362-B5B7-C0E7E1916F69Q30484982-0381859D-8D02-4493-AEE0-58D0E788536BQ30501294-74DAC7F3-7A42-4DC7-9998-F0059B66560EQ30503656-D1DEA4A3-EB1F-460A-9EA7-2C0F926A098FQ36458218-9DE9D8CF-E310-4333-A5E5-FC7889EC154EQ37602435-D6F7526D-403C-4384-B4A2-CA6C3FEAB734Q37602851-DBE243BF-D78D-4600-87BF-69B4D6CF21A9Q39748517-F474BF9F-F6DA-41E6-B885-398AA15D1AFCQ40154461-D6D8715A-9DFA-4038-9EF7-A14256E72AA9Q41774711-90E2AA57-F152-4E44-9C3A-84FD08BA42F3Q41858684-81083617-DE9B-4C72-9AE2-3475AF2F1254Q42545972-EBC6F4C2-BA4C-4BF3-ADF6-4FF842AF372BQ42841808-D30C1964-0F52-4586-99C7-5685417F510DQ43754797-AF6B7A9B-33F6-4989-952A-2B06A01CA51DQ55313128-9BE51E3D-B944-4025-8616-5FC370144281Q57133493-55CCB012-1E57-47F4-A028-AECCA36FD42EQ58824039-3D526ACD-99C6-49C5-ADB5-BADB58B17420
P2860
Increase in apparent compressibility of cytochrome c upon oxidation.
description
1982 nî lūn-bûn
@nan
1982年の論文
@ja
1982年学术文章
@wuu
1982年学术文章
@zh-cn
1982年学术文章
@zh-hans
1982年学术文章
@zh-my
1982年学术文章
@zh-sg
1982年學術文章
@yue
1982年學術文章
@zh
1982年學術文章
@zh-hant
name
Increase in apparent compressibility of cytochrome c upon oxidation.
@ast
Increase in apparent compressibility of cytochrome c upon oxidation.
@en
type
label
Increase in apparent compressibility of cytochrome c upon oxidation.
@ast
Increase in apparent compressibility of cytochrome c upon oxidation.
@en
prefLabel
Increase in apparent compressibility of cytochrome c upon oxidation.
@ast
Increase in apparent compressibility of cytochrome c upon oxidation.
@en
P2093
P2860
P356
P1476
Increase in apparent compressibility of cytochrome c upon oxidation.
@en
P2093
P2860
P304
P356
10.1073/PNAS.79.3.815
P407
P577
1982-02-01T00:00:00Z