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Anilino Naphthalenesulfonates (0):
Recent article
Anilino Naphthalenesulfonates
Abstract
We observed that at higher pH, BSF exists in alkaline unfolded state. Our results provided evidence that correlates simultaneous formation of secondary structure followed by accumulation of hydrophobic clusters....
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PMID: 19995341
PDF is available here.
PDF is available here.
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Abstract
Penicillin amidase from Alacaligenes faecalis is an attractive biocatalyst for hydrolysis of penicillin G for production of 6-aminopenicillanic acid, which is used in the synthesis of semi-synthetic beta-lactam antibiotics. Recently a mutant of this enzyme with extended C-terminus of the A-chain com...
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PMID: 20224955
PDF is available here.
PDF is available here.
Molecular Endocrinology (23)8 2009
Abstract
We used steady-state second-derivative absorption and emission spectroscopy, pressure and temperature perturbations, and 4,4'-bis-anilinonaphthalene 8-sulfonate (bis-ANS) partitioning to determine the kinetics and thermodynamics of the conformational changes in AR-LBD after dihydrotestosterone (DHT)...
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PMID: 19443608
PDF is available here.
PDF is available here.
Biochemistry (Washington) (48)30 2009
Abstract
I [betaB1(99-252)], N-terminal arm + motif I + motif II [betaB1(144-252)], N-terminal arm + motif I + motif II + connecting peptide [betaB1(149-252)], C-terminal extension [betaB1(1-234)], C-terminal extension plus motif IV [betaB1(1-190)], or C-terminal extension + motif III + motif IV [betaB1(1-14...
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PMID: 19548648
PDF is available here.
PDF is available here.
Abstract
A system for studying biological effect of radio frequency electromagnetic field was developed. The system can form an area where electromagnetic wave with large frequency range is well distributed. The strength of electromagnetic wave was measured easily. Electromagnetic wave in the system did not...
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PMID: 19798972
PDF is available here.
PDF is available here.
Abstract
We have investigated the organization and dynamics of tryptophan residues in tetrameric, monomeric and unfolded states of soybean agglutinin (SBA) by selective chemical modification, steady-state and time-resolved fluorescence, and phosphorescence. Oxidation with N-bromosuccinimide (NBS) modifies tw...
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PMID: 19383525
PDF is available here.
PDF is available here.
Abstract
We have investigated the organization and dynamics of tryptophan residues in tetrameric, monomeric and unfolded states of soybean agglutinin (SBA) by selective chemical modification, steady-state and time-resolved fluorescence, and phosphorescence. Oxidation with N-bromosuccinimide (NBS) modifies tw...
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PMID: 19383525
PDF is available here.
PDF is available here.
Abstract
We have investigated the organization and dynamics of tryptophan residues in tetrameric, monomeric and unfolded states of soybean agglutinin (SBA) by selective chemical modification, steady-state and time-resolved fluorescence, and phosphorescence. Oxidation with N-bromosuccinimide (NBS) modifies tw...
|
PMID: 19383525
PDF is available here.
PDF is available here.
Abstract
We have investigated the organization and dynamics of tryptophan residues in tetrameric, monomeric and unfolded states of soybean agglutinin (SBA) by selective chemical modification, steady-state and time-resolved fluorescence, and phosphorescence. Oxidation with N-bromosuccinimide (NBS) modifies tw...
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PMID: 19383525
PDF is available here.
PDF is available here.
Abstract
We have investigated the organization and dynamics of tryptophan residues in tetrameric, monomeric and unfolded states of soybean agglutinin (SBA) by selective chemical modification, steady-state and time-resolved fluorescence, and phosphorescence. Oxidation with N-bromosuccinimide (NBS) modifies tw...
|
PMID: 19383525
PDF is available here.
PDF is available here.
Abstract
We have investigated the organization and dynamics of tryptophan residues in tetrameric, monomeric and unfolded states of soybean agglutinin (SBA) by selective chemical modification, steady-state and time-resolved fluorescence, and phosphorescence. Oxidation with N-bromosuccinimide (NBS) modifies tw...
|
PMID: 19383525
PDF is available here.
PDF is available here.
Abstract
We have investigated the organization and dynamics of tryptophan residues in tetrameric, monomeric and unfolded states of soybean agglutinin (SBA) by selective chemical modification, steady-state and time-resolved fluorescence, and phosphorescence. Oxidation with N-bromosuccinimide (NBS) modifies tw...
|
PMID: 19383525
PDF is available here.
PDF is available here.
Abstract
We have investigated the organization and dynamics of tryptophan residues in tetrameric, monomeric and unfolded states of soybean agglutinin (SBA) by selective chemical modification, steady-state and time-resolved fluorescence, and phosphorescence. Oxidation with N-bromosuccinimide (NBS) modifies tw...
|
PMID: 19383525
PDF is available here.
PDF is available here.
Abstract
We have investigated the organization and dynamics of tryptophan residues in tetrameric, monomeric and unfolded states of soybean agglutinin (SBA) by selective chemical modification, steady-state and time-resolved fluorescence, and phosphorescence. Oxidation with N-bromosuccinimide (NBS) modifies tw...
|
PMID: 19383525
PDF is available here.
PDF is available here.
Abstract
We have investigated the organization and dynamics of tryptophan residues in tetrameric, monomeric and unfolded states of soybean agglutinin (SBA) by selective chemical modification, steady-state and time-resolved fluorescence, and phosphorescence. Oxidation with N-bromosuccinimide (NBS) modifies tw...
|
PMID: 19383525
PDF is available here.
PDF is available here.
Abstract
We have investigated the organization and dynamics of tryptophan residues in tetrameric, monomeric and unfolded states of soybean agglutinin (SBA) by selective chemical modification, steady-state and time-resolved fluorescence, and phosphorescence. Oxidation with N-bromosuccinimide (NBS) modifies tw...
|
PMID: 19383525
PDF is available here.
PDF is available here.
Abstract
We have investigated the organization and dynamics of tryptophan residues in tetrameric, monomeric and unfolded states of soybean agglutinin (SBA) by selective chemical modification, steady-state and time-resolved fluorescence, and phosphorescence. Oxidation with N-bromosuccinimide (NBS) modifies tw...
|
PMID: 19383525
PDF is available here.
PDF is available here.
Abstract
We have investigated the organization and dynamics of tryptophan residues in tetrameric, monomeric and unfolded states of soybean agglutinin (SBA) by selective chemical modification, steady-state and time-resolved fluorescence, and phosphorescence. Oxidation with N-bromosuccinimide (NBS) modifies tw...
|
PMID: 19383525
PDF is available here.
PDF is available here.
Abstract
We have investigated the organization and dynamics of tryptophan residues in tetrameric, monomeric and unfolded states of soybean agglutinin (SBA) by selective chemical modification, steady-state and time-resolved fluorescence, and phosphorescence. Oxidation with N-bromosuccinimide (NBS) modifies tw...
|
PMID: 19383525
PDF is available here.
PDF is available here.
Abstract
We have investigated the organization and dynamics of tryptophan residues in tetrameric, monomeric and unfolded states of soybean agglutinin (SBA) by selective chemical modification, steady-state and time-resolved fluorescence, and phosphorescence. Oxidation with N-bromosuccinimide (NBS) modifies tw...
|
PMID: 19383525
PDF is available here.
PDF is available here.
Abstract
We have investigated the organization and dynamics of tryptophan residues in tetrameric, monomeric and unfolded states of soybean agglutinin (SBA) by selective chemical modification, steady-state and time-resolved fluorescence, and phosphorescence. Oxidation with N-bromosuccinimide (NBS) modifies tw...
|
PMID: 19383525
PDF is available here.
PDF is available here.
Biochemistry (Washington) (48)18 2009
Abstract
We have recently proposed. They also suggest that it is possible to engineer a Ca(2+)-dependent conformational change into a high-affinity EF-hand protein, furnishing a mechanism by which the protein could play a reverse Ca(2+) sensor role....
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PMID: 19290658
PDF is available here.
PDF is available here.
Methods in Molecular Biology (543)543 2009
Abstract
We make use of an extrinsic fluorescence probe, the environmentally sensitive fluorophore 1-anilinonaphthalene-8-sulphonic acid (1,8-ANS). Displacement by DNA of 1,8-ANS molecules from the nucleic-acid-binding site of the Type I modification methylase EcoR124I results in red shifting and an intensit...
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PMID: 19378188
PDF is available here.
PDF is available here.
Biochemical Journal (419)2 2009
Abstract
These results indicate that MsbA contains two substrate-binding sites that communicate with both the nucleotide-binding domain and with each other. One is a high affinity binding site for the physiological substrate, lipid A, and the other site interacts with drugs with comparable affinity. Thus Msb...
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PMID: 19132955
PDF is available here.
PDF is available here.
Journal of Fluorescence (19)2 2009
Abstract
Dendrimers have been proposed as new carriers for drug delivery. They have distinctive characteristics, such as uniform and controlled size, monodispersity and modifiable surface group functionality, which make them extremely useful for biomedical applications. In this study, the binding capacity of...
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PMID: 18758926
PDF is available here.
PDF is available here.
Abstract
Peroxynitrite is an extremely reactive entity and has in vivo existence. Its interaction with biomolecules may cause oxidation and nitration. In this study, commercially available H2A histone was exposed to peroxynitrite generated in vitro. The peroxynitrite-mediated structural changes in histone we...
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PMID: 19144075
PDF is available here.
PDF is available here.
Effect of Charge Distribution in a Flexible Loop on the Bioluminescence Color of Firefly Luciferases
Abstract
Firefly luciferase is a monooxygenase that catalyzes the ATP-dependent conversion of firefly luciferin into a luciferyl-adenylate, which is oxidized to an electronically excited oxyluciferin in a multistep reaction and produces visible light with a remarkable quantum yield. The bioluminescence color...
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PMID: 19119851
PDF is available here.
PDF is available here.
Analytical Sciences (25)1 2009
Binding Properties of Hydrophobic Molecules to Human Serum Albumin Studied by Fluorescence Titration
Abstract
Two fluorescence modes were combined to analyze the binding properties of terminally substituted alkanes (C(n)X, X = COOH, OH, CHO, NH(2)) to human serum albumin (HSA). A competitive binding assay using an 8-anilino-1-naphthalenesulfonate (ANS) fluorescence probe provides information on all the hydr...
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PMID: 19139584
PDF is available here.
PDF is available here.
Protein Science (12)10 2009
Abstract
Chemical modification of Torpedo californica acetylcholinesterase by the natural thiosulfinate allicin produces an inactive enzyme through reaction with the buried cysteine Cys 231. Optical spectroscopy shows that the modified enzyme is ldquonative-like,rdquo and inactivation can be reversed by expos...
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PMID: 14500892
PDF is available here.
PDF is available here.
Plant, Cell & Environment (31)12 2008
Abstract
We have termed hydrophilins. Previously, we showed that hydrophilins protect enzyme activities in vitro from low water availability effects. Here, we demonstrate that hydrophilins can also protect enzyme activities from the adverse effects induced by freeze-thaw cycles in vitro. We monitored conform...
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PMID: 18761701
PDF is available here.
PDF is available here.
Journal of Biological Chemistry (283)45 2008
Abstract
We have purified functional B. subtilis SepF from the inclusion bodies overexpressed in Escherichia coli. Far-UV circular dichroism and fluorescence spectroscopic analysis involving the extrinsic fluorescent probe 1-anilinonaphthalene-8-sulfonic acid suggested that the purified SepF had characterist...
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PMID: 18782755
PDF is available here.
PDF is available here.
Journal of Molecular Biology (382)5 2008
Abstract
We used a 4,4'-dianilino-1,1'-binaphthyl-5,5'-disulfonic acid (BisANS) photolabeling approach to monitor changes in protein unfolding in vivo in skeletal muscle proteins in ALS mice. We find two major proteins, creatine kinase (CK) and glyceraldehyde-3-phosphate dehydrogenase (GAPDH), conformational...
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PMID: 18706911
PDF is available here.
PDF is available here.
Journal of Biological Chemistry (283)42 2008
Abstract
We employed novel mass spectrometry techniques to investigate the changes in quaternary structure associated with this switch from chaperone to adjuvant of aggregation. We replicated the oligomeric rearrangements observed for post-translationally modified alpha-crystallins, without altering the prot...
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PMID: 18713743
PDF is available here.
PDF is available here.
Abstract
Mechanism of interaction of antidiabetic drugs, repaglinide and gliclazide, to human serum albumin has been studied using fluorescence spectroscopic technique. Repaglinide had much higher affinity for human serum albumin when compared with gliclazide. The order of association constants was 10(5) for...
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PMID: 18844675
PDF is available here.
PDF is available here.
Biophysical Chemistry (137)2-3 2008
Abstract
Molecular docking and ANS-displacement experiments indicated that 8-anilinonaphthalene sulfonate (ANS) binds the hydrophobic site (H-site) in the active site of dimeric class Mu rGST M1-1. The naphthalene moiety provides most of the van der Waals contacts at the ANS-binding interface while the anili...
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PMID: 18703268
PDF is available here.
PDF is available here.
Journal of Biochemistry (144)4 2008
Abstract
These results suggest that the structure of alpha-momorcharin holds the more compact conformation as an incipient state for unfolding, which is the sharp contrast to beta-momorcharin that gives the characteristics of the generally known molten globule state....
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PMID: 18603588
PDF is available here.
PDF is available here.
Journal of Molecular Biology (381)5 2008
Abstract
We have investigated the aggregation and amyloid fibril formation of bovine beta-lactoglobulin variant A, with a focus on the early stages of aggregation. We used noncovalent labeling with thioflavin T and 1-anilino-8-naphthalenesulfonate to follow the conformational changes occurring in beta-lactog...
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PMID: 18590743
PDF is available here.
PDF is available here.
Biochimica et Biophysica Acta (1784)9 2008
Abstract
These results were correlated with secondary and tertiary structure changes assessed by the CD spectrum and fluorescence of the single tryptophan and the six tyrosine residues. The WT cutinase and S54D variant have similar secondary and tertiary structures that differ from those of T179C and L153Q v...
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PMID: 18501723
PDF is available here.
PDF is available here.
Abstract
We suggest that Co2+ may bind with some amino acids near or in the active site of HRP and the conformational changes of HRP induced by such binding should be the main reason for activation and inactivation effect of Co2+. The potential binding sites of Co2+ were also proposed....
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PMID: 18533729
PDF is available here.
PDF is available here.
Biophysical Chemistry (136)2-3 2008
Abstract
The association behavior of casein over a broad pH range has first been investigated by fluorescent technique together with DLS and turbidity measurements. Casein molecules can self-assemble into casein micelles in the pH ranges 2.0 to 3.0, and 5.5 to 12.0. The hydrophobic interaction, hydrogen bond...
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PMID: 18583019
PDF is available here.
PDF is available here.
Abstract
The solvatochromic fluorescent probe 8-anilino-1-naphthalenesulfonate (ANS) has been used to study the hydrophobicity and conformational dynamics of lecithin:cholesterol acyltransferase (LCAT). The ANS to LCAT binding constant was estimated from titrations with ANS, keeping a constant concentration...
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PMID: 18485727
PDF is available here.
PDF is available here.
Abstract
Liver-fatty acid binding protein (L-FABP) is found in high levels in enterocytes and is involved in the cytosolic solubilization of fatty acids during fat absorption. In the current studies, the interaction of L-FABP with a range of lipophilic drugs has been evaluated to explore the potential for L-...
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PMID: 18533710
PDF is available here.
PDF is available here.
Abstract
The effect of bulk-phase pH on the apparent affinity (K(d)(app)) of purified wild-type lactose permease (LacY) for sugars was studied. K(d)(app) values were determined by ligand-induced changes in the fluorescence of either of two covalently bound fluorescent reporters positioned away from the sugar...
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PMID: 18567672
PDF is available here.
PDF is available here.
Abstract
We analyzed the binding efficiency of Cu and Fe to alpha-synuclein by fluorescence studies. It is interesting to note that Cu and Fe showed differential binding pattern toward alpha-synuclein (wild type and A30P, A53T, and E46K mutant forms) as revealed by intrinsic tyrosine fluorescence, thioflavin...
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PMID: 18491043
PDF is available here.
PDF is available here.
Abstract
We determined the DNA-binding surface of the STPR third repeat (R3) by alanine scanning mutagenesis; a particular site, composed of hydrophobic and hydrophilic residues, was identified. Notably, the substitution of Arg-9 in R3 with alanine residue, which is located in the middle of the surface, dras...
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PMID: 18214959
PDF is available here.
PDF is available here.
Biochemistry (Washington) (47)22 2008
Abstract
The binding of the inner membrane insertase YidC from Escherichia coli to its substrate, the Pf3 coat protein, was examined in vitro by fluorescence spectroscopy. Purified YidC protein was solubilized with the lipid-like detergent n-dodecylphosphocholine and noncovalently labeled with 1-anilino-naph...
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PMID: 18457424
PDF is available here.
PDF is available here.
Abstract
We investigated the effect of ageing on oxidative damage of protein amino acid residues and lipids in heart homogenate and mitochondria of 4- and 26-month-old Wistar rats. Levels of dityrosine and levels of lysine conjugates increased in heart homogenate during ageing, although levels of conjugated...
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PMID: 18645226
PDF is available here.
PDF is available here.
Abstract
Many pathogenic gram-negative bacteria employ type III secretion systems to transport proteins into the host cell membrane and cytoplasm to subvert normal cellular functions. The type III secretion apparatus consists of a basal body spanning the inner and outer bacterial membranes and a needle which...
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PMID: 18175320
PDF is available here.
PDF is available here.
Abstract
Beta-casein (beta-CN) showing properties of intrinsically unstructured proteins (IUP) displays many similarities with molecular chaperones and shows anti-aggregation activity in vitro. Chaperone activities of bovine and camel beta-CN were studied using alcohol dehydrogenase (ADH) as a substrate. To...
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PMID: 18336901
PDF is available here.
PDF is available here.
Protein Science (17)5 2008
Abstract
We have investigated the role of the lone cysteine residue in the assembly of MtbFtsZ using different complimentary approaches, namely chemical modification by a thiol-specific reagent 5,5'-dithiobis-(2-nitrobenzoic acid) (DTNB) or a cysteine-chelating agent HgCl(2), and site-directed mutagenesis of...
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PMID: 18436955
PDF is available here.
PDF is available here.
Protein Science (17)4 2008
Abstract
We obtained detailed information on ANS-protein interactions in the absence and presence of urea. The effects of ambient to elevated temperatures on the affinity and specificity of ANS binding were assessed from experiments performed at 25 degrees C and 37 degrees C. Overall, the affinity of ANS was...
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PMID: 18305195
PDF is available here.
PDF is available here.
Biochemistry (New York) (73)4 2008
Abstract
Using steady-state, polarized, and phase-modulation fluorometry, the dithiothreitol-induced denaturation of insulin and formation of its complex with alpha-crystallin in solution were studied. Prevention of the aggregation of insulin by alpha-crystallin is due to formation of chaperone complexes, i....
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PMID: 18457576
PDF is available here.
PDF is available here.
Journal of Molecular Biology (377)3 2008
Abstract
We report the first NMR-based solution structural data for the CT enzymatic domain (CTA1). We show that this free enzymatic domain partially unfolds at the C-terminus and binds its protein partners at both the beginning and the end of this activation process. Deviations from random coil chemical shi...
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PMID: 18272180
PDF is available here.
PDF is available here.
Biochemistry (Washington) (47)11 2008
Abstract
We have shown this region has the propensity to form alpha-helix structure. Significantly, the binding of specific protein targets or a natural osmolyte resulted in a more protease resistant conformation for the AF1 domain, consistent with an increase in conformational stability. Computational and e...
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PMID: 18284208
PDF is available here.
PDF is available here.
Journal of Biological Chemistry (283)11 2008
Abstract
We generated and characterized C-terminal truncated, double ring, and single ring mutants of GroEL. The ability to assist the refolding of substrate proteins rhodanese and malate dehydrogenase decreased suddenly when 23 amino acids were truncated, indicating that a sudden change in the environment w...
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PMID: 18184659
PDF is available here.
PDF is available here.
Journal of Fluorescence (18)2 2008
Abstract
Determination of binding parameters such as the number of ligands and the respective binding constants require a considerable number of experiments to be performed. These involve accurate determination of either free and/or bound ligand concentration irrespective of the measurement technique applied...
|
PMID: 18097738
PDF is available here.
PDF is available here.
Journal of Fluorescence (18)2 2008
Abstract
The saccharide binding and conformational characterization of a hemagglutinin, a low molecular weight protein from the seeds of Moringa oleifera was studied using steady state and time resolved fluorescence. The lectin binds sugars LacNAc (K (a) = 1380 M(-1)) and fructose (K (a) = 975 M(-1)), as det...
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PMID: 18046633
PDF is available here.
PDF is available here.
Abstract
We capitalized on the hydrophobic and hydrophilic properties of 8-anilino-1-naphthalenesulfonic acid (ANS). In single Trp mutants, resonance energy transfer from Trp to ANS indicates that the naphthalene group of ANS is proximate to Leu105 in the cavity. Binding energies of TL to ANS and its analogu...
|
PMID: 18179255
PDF is available here.
PDF is available here.
Abstract
ZnuA is the periplasmic Zn(2+)-binding protein associated with the high-affinity ATP-binding cassette ZnuABC transporter from Escherichia coli. Although several structures of ZnuA and its homologs have been determined, details regarding metal ion stoichiometry, affinity, and specificity as well as t...
|
PMID: 18027003
PDF is available here.
PDF is available here.
Abstract
We present results of in vitro experiments that show bivalent zinc specifically interacts with alpha-crystallin with a dissociation constant in the submillimolar range (Kd approximately 0.2-0.4 mM). We compared the effect of Zn2+ with those of Ca2+, Cu2+, Mg2+, Cd2+, Pb2+, Ni2+, Fe2+, and Co2+ at 1...
|
PMID: 18095658
PDF is available here.
PDF is available here.