4-(2-碘代乙酰氨基)-2,2,6,6-四甲基哌啶-1-氧基自由基结构式
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常用名 | 4-(2-碘代乙酰氨基)-2,2,6,6-四甲基哌啶-1-氧基自由基 | 英文名 | 4-(2-iodoacetamido)-tempo |
|---|---|---|---|---|
| CAS号 | 25713-24-0 | 分子量 | 339.193 | |
| 密度 | 1.53g/cm3 | 沸点 | 428.8ºC at 760mmHg | |
| 分子式 | C11H20IN2O2 | 熔点 | 114-117ºC | |
| MSDS | 中文版 美版 | 闪点 | 213.1ºC | |
| 符号 |
GHS07 |
信号词 | Warning |
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A paramagnetic molecular voltmeter.
J. Magn. Reson. 190(1) , 7-25, (2008) We have developed a general electron paramagnetic resonance (EPR) method to measure electrostatic potential at spin labels on proteins to millivolt accuracy. Electrostatic potential is fundamental to energy-transducing proteins like myosin, because molecular ... |
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Electron-electron spin-spin interaction in spin-labeled low-spin methemoglobin.
Biophys. J. 68(6) , 2531-42, (1995) Nitroxyl free radical electron spin relaxation times for spin-labeled low-spin methemoglobins were measured between 6 and 120 K by two-pulse electron spin echo spectroscopy and by saturation recovery electron paramagnetic resonance (EPR). Spin-lattice relaxat... |
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Phosphorylation regulates the ADP-induced rotation of the light chain domain of smooth muscle myosin.
Biochemistry 38(31) , 10107-18, (1999) We have observed the effects of MgADP and thiophosphorylation on the conformational state of the light chain domain of myosin in skinned smooth muscle. Electron paramagnetic resonance (EPR) spectroscopy was used to monitor the orientation of spin probes attac... |
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An iodoacetamide spin-label selectively labels a cysteine side chain in an occluded site on the sarcoplasmic reticulum Ca(2+)-ATPase.
Biochemistry 32(40) , 10803-11, (1993) Sarcoplasmic reticulum vesicles were labeled with [14C]iodoacetamide spin-label (ISL) under conditions where time courses of the reaction predicted that one amino acid residue would be preferentially labeled. Solubilized tryptic peptides were separated by hig... |
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Resolved conformational states of spin-labeled Ca-ATPase during the enzymatic cycle.
Biochemistry 31(32) , 7381-9, (1992) We have used frequency- and time-resolved electron paramagnetic resonance (EPR) to study the effects of substrate on the nanosecond conformational dynamics of the Ca-ATPase of sarcoplasmic reticulum, as detected by an iodoacetamide spin label (IASL) attached ... |
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The characterization of vanadate-trapped nucleotide complexes with spin-labelled myosins.
J. Muscle Res. Cell Motil. 5(1) , 97-112, (1984) The properties of spin-labelled myosin, prepared from rabbit skeletal and scallop adductor muscle, on forming a long-lived complex with ADP and vanadate (M.ADP.Vi), have been investigated. In the case of an iodoacetamide-based label attached to rabbit myosin ... |
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The mobility of troponin C and troponin I in muscle.
J. Mol. Recognit. 10(4) , 194-201, (1997) In vertebrate skeletal muscle, contraction is initiated by the elevation of the intracellular Ca2+ concentration. The binding of Ca2+ to TnC induces a series of conformational changes which ultimately release the inhibition of the actomyosin ATPase activity b... |
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Dynamic aspects of the incorporation of proteins into biological membranes.
J. Mol. Recognit. 10(4) , 188-93, (1997) The contributions of intramembranous and extramembranous segments of transmembrane proteins to frictional forces have been studied by covalently attached 14N- and 15N-indane dione and maleimide spin labels using saturation transfer electron spin resonance spe... |
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Pressure induced structural fluctuations in hemoglobin, studied by EPR-spectroscopy.
Z. Naturforsch., C, J. Biosci. 43(3-4) , 162-6, (1988) A quartz based cavity for pressure dependent EPR measurements on liquid samples allowing pressures up to 0.6 GPa was constructed. First investigations with this setup were done on spin labeled horse hemoglobin derivatives both in ferric and ferrous state of o... |
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Effect of hyperthermia and ionizing radiation on the erythrocyte membrane.
Int. J. Radiat. Biol. Relat. Stud. Phys. Chem. Med. 42(1) , 45-55, (1982) Spin-label studies of the effects of hyperthermia on the erythrocyte membrane revealed a decrease in the fluidity of lipids and changes in the state of membrane proteins. The rate of haemolysis in iso-osmotic glycerol solution was increased. Changes of most o... |