7-氮杂色氨酸一水合物
7-氮杂色氨酸一水合物结构式
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常用名 | 7-氮杂色氨酸一水合物 | 英文名 | 7-azatryptophan |
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| CAS号 | 7303-50-6 | 分子量 | 205.213 | |
| 密度 | 1.4±0.1 g/cm3 | 沸点 | 466.1ºC at 760 mmHg | |
| 分子式 | C10H11N3O2 | 熔点 | 275°C dec. | |
| MSDS | 美版 | 闪点 | 235.7ºC |
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Phosphorescence and optically detected magnetic resonance characterization of the environments of tryptophan analogues in staphylococcal nuclease, its V66W mutant, and Delta 137-149 fragment.
Biochemistry 37(25) , 8954-64, (1998) Phosphorescence and optically detected magnetic resonance (ODMR) measurements are reported on the triplet states of the tryptophan analogues, 7-azatryptophan (7AW), 5-hydroxytryptophan (5HW), and 4-, 5-, and 6-fluorotryptophan (4FW, 5FW, 6FW), when incorporat... |
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Blue fluorescent amino acids as in vivo building blocks for proteins.
ChemBioChem. 11(3) , 305-14, (2010) In vivo expression of colored proteins without post-translational modification or chemical functionalization is highly desired for protein studies and cell biology. Cell-permeable tryptophan analogues, such as azatryptophans, have proved to be almost ideal is... |
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In vivo properties of thiol inhibitors of the three vasopeptidases NEP, ACE and ECE are improved by introduction of a 7-azatryptophan in P2' position.
J. Pept. Res. 63(2) , 99-107, (2004) Three zinc metallopeptidases are implicated in the regulation of fluid homeostasis and vascular tone and represent interesting targets for the treatment of chronic heart failure. We have previously reported the synthesis of a triple inhibitor able to simultan... |
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Biosynthetic incorporation of tryptophan analogues into staphylococcal nuclease: effect of 5-hydroxytryptophan and 7-azatryptophan on structure and stability.
Protein Sci. 6(3) , 689-97, (1997) 5-Hydroxytryptophan (5HW) and 7-azatryptophan (7AW) are analogue of tryptophan that potentially can be incorporated biosynthetically into proteins and used as spectroscopic probes for studying protein-DNA and protein-protein complexes. The utility of these pr... |
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Incorporation of the fluorescent amino acid 7-azatryptophan into the core domain 1-47 of hirudin as a probe of hirudin folding and thrombin recognition.
Protein Sci. 13(6) , 1489-502, (2004) 7-Azatryptophan (AW), a noncoded isostere of tryptophan (W), possesses interesting spectral properties. In particular, the presence of a nitrogen atom at position 7 in the indolyl nucleus of AW results in a red shift of the absorption maximum and fluorescence... |
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Influence of steric bulk and electrostatics on the hydroxylation regiospecificity of tryptophan hydroxylase: characterization of methyltryptophans and azatryptophans as substrates.
Biochemistry 38(49) , 16283-9, (1999) Tryptophan hydroxylase is a pterin-dependent amino acid hydroxylase that catalyzes the incorporation of one atom of molecular oxygen into tryptophan to form 5-hydroxytryptophan. The substrate specificity and hydroxylation regiospecificity of tryptophan hydrox... |
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Characterization of the fluorescence emission properties of 7-azatryptophan in reverse micellar environments.
Biochem. Biophys. Res. Commun. 219(2) , 388-92, (1996) The amino acid analogue 7-azatryptophan has attracted significant recent attention as a novel optical probe for protein structure, function and dynamics. We report here, for the first time, its fluorescence emission behavior in a membrane mimetic model system... |
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A concerted structural transition in the plasminogen activator inhibitor-1 mechanism of inhibition.
Biochemistry 41(40) , 11997-2009, (2002) The inhibition mechanism of serpins requires a change in structure to entrap the target proteinase as a stable acyl-enzyme complex. Although it has generally been assumed that reactive center loop insertion and associated conformational change proceeds in a c... |
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Azatryptophans as tools to study polarity requirements for folding of green fluorescent protein.
J. Pept. Sci. 16(10) , 589-95, (2010) Aequorea victoria green fluorescent protein and its widely used mutants enhanced green fluorescent protein and enhanced cyan fluorescent protein (ECFP) are ideal target proteins to study protein folding. The spectral signals of their chromophores are directly... |
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Catalytic folding of the Cepsilon3 domain by its high affinity receptor.
FEBS Lett. 580(8) , 2129-34, (2006) The interaction of immunoglobulin E (IgE) with its cellular receptor FcepsilonRIalpha is a central regulator of allergy. Structural studies have identified the third domain (Cepsilon3) of the constant region of epsilon heavy chain as the receptor binding regi... |