8-[2-[(2-iodoacetyl)amino]ethylamino]naphthalene-1-sulfonic acid
![8-[2-[(2-iodoacetyl)amino]ethylamino]naphthalene-1-sulfonic acid Structure](https://image.chemsrc.com/caspic/227/36930-64-0.png)
8-[2-[(2-iodoacetyl)amino]ethylamino]naphthalene-1-sulfonic acid structure
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Common Name | 8-[2-[(2-iodoacetyl)amino]ethylamino]naphthalene-1-sulfonic acid | ||
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| CAS Number | 36930-64-0 | Molecular Weight | 434.24900 | |
| Density | 1.808 g/cm3 | Boiling Point | N/A | |
| Molecular Formula | C14H15IN2O4S | Melting Point | 198-200ºC | |
| MSDS | N/A | Flash Point | N/A | |
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Conformational distributions and proximity relationships in the rigor complex of actin and myosin subfragment-1.
J. Biol. Chem. 275(4) , 2404-9, (2000) Cyclic conformational changes in the myosin head are considered essential for muscle contraction. We hereby show that the extension of the fluorescence resonance energy transfer method described originally by Taylor et al. (Taylor, D. L., Reidler, J., Spudich... |
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Hairpin configuration of H-2Kk in liposomes formed by detergent dialysis.
Biochemistry 23(19) , 4401-9, (1984) H-2Kk is a transmembrane glycoprotein having the N-terminal region of the heavy chain exposed at the cell surface and the C-terminal region exposed at the cytoplasmic face in its native configuration in the plasma membrane. The configuration of H-2Kk in lipos... |
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Assignment of free and disulfide-bonded cysteine residues in testis angiotensin-converting enzyme: functional implications.
Biochemistry 35(29) , 9560-6, (1996) Human testicular angiotensin-converting enzyme (tACE) is an extracellular protein that contains seven cysteine residues. The cysteines occur in a sequential distribution that is precisely mimicked in the tACE from rabbit and mouse, and in both domains of all ... |
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Vectorially oriented monolayers of detergent-solubilized Ca(2+) -ATPase from sarcoplasmic reticulum.
Biophys. J. 70(5) , 2131-43, (1996) A method for tethering proteins to solid surfaces has been utilized to form vectorially oriented monolayers of the detergent-solubilized integral membrane protein Ca(2+) -ATPase from the sarcoplasmic reticulum (SR). Bifunctional, organic self-assembled monola... |
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SH1 (cysteine 717) of smooth muscle myosin: its role in motor function.
Biochemistry 38(36) , 11670-6, (1999) To determine if a thiol group called SH1 has an important role in myosin's motor function, we made a mutant heavy meromyosin (HMM) without the thiol group and analyzed its properties. In chicken gizzard myosin, SH1 is located on the cysteine residue at positi... |
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Replacement of ATP with ADP affects the dynamic and conformational properties of actin monomer.
Biochemistry 38(39) , 12885-92, (1999) The effect of the replacement of ATP with ADP on the conformational and dynamic properties of the actin monomer was investigated, by means of electron paramagnetic resonance (EPR) and fluorescence spectroscopic methods. The measurement of the ATP concentratio... |
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Energy-transfer measurements on a double fluorescent labeled ribonuclease A.
Biochemistry 22(16) , 3829-36, (1983) Two fluorescent groups have been covalently attached to ribonuclease A: first, the alpha-amino group is labeled upon reaction with fluorescein isothiocyanate, and second, one of the active site histidine residues is modified by N-[[(iodoacetyl)amino]ethyl]-5-... |
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N-terminal domain unfolds first in the sequential unfolding of papain.
Protein Pept. Lett. 10(1) , 83-90, (2003) Temperature and Guanidine hydrochloride induced unfolding transitions of papain at pH 2.0 are biphasic implying independent and sequential unfolding of its two domains. To determine the order of unfolding, the active site located in the interface of the domai... |
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Site-specific modification or rabbit muscle aldolase with fluorescent probes.
Acta Biochim. Pol. 37(4) , 463-74, (1990) The site-specific modification of rabbit muscle aldolase A by labeling of thiol residues of Cys-289 with 5-(2-((iodoacetyl)amino)ethyl)amino)naphthalene-1-sulfonic acid and Cys-239 with 5-iodoacetamidofluorescein or 4-dimethylamino-phenylazophenyl-4'-maleimid... |
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Effect of histone H3 sulfhydryl modifications on histone-histone interactions and nucleosome formation and structure.
Eur. J. Biochem. 109(2) , 369-76, (1980) The effect of histone H3 sulfhydryl mnodification and disulfide bridge formation on histone-histone interactions, nucleosome reconstitution and structure has been examined for calf and chicken mononucleosomes. For intramolecular disulfide bridge formation his... |