• Journal of the Korean Magnetic Resonance Society
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• v.17 no.2
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• pp.76-80
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• 2013

The TCP domain is a DNA-binding domain present in plant transcription factors and has a similar structural feature to the bHTH motif of eukaryotic transcription factors. The imino proton exchange study has been performed for the DNA duplex containing the consensus DNA-binding site for the AtTCP11 transcription factor. The first two base pairs in the consensus 5'-GTGGG-3' sequence are relatively very unstable but lead to greater stabilization of the neighboring two G C base pairs. These unique dynamic features of the five base pairs in the consensus DNA sequence might play crucial roles in the effective DNA binding of the AtTCP11 protein.

• Clinical and Experimental Reproductive Medicine
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• v.18 no.1
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• pp.23-34
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• 1991

In order to study the sperm-egg interaction during fertilization process in mouse, the effects of sperm concentration, the duration of capacitation and insemination, the stages of maturation and development of eggs, and sperm extracts and BSA on sperm binding to egg were examined. Sperm-egg binding was increased depending on sperm concentration within the range of $10^3-10^6$ sperm/ml. It showed the most numbers of sperm-egg binding at 60min from the beginning of preincubation(capacitation) and insemination, respectively. During sperm capacitation, sperm-egg binding inhibitor was released from sperm into the incubation medium. Sperm extracts containing trypsin-like enzyme which is secreted through the acrosome reaction increased the binding. BSA in the culture medium showed a positive effect on the binding. It is suggested that physicochemical alterations of zona pellucida in the process of maturation and fertilization of eggs leaded to inhibition of sperm-egg binding.

• BMB Reports
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• v.29 no.6
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• pp.525-529
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• 1996

Ligand binding properties of muscarinic acetylcholine receptors (mAChRs) in the nematode Caenorhabditis elegans (C. elegans) were characterized by using filtration binding assays. Scatchard analysis using $[^{3}H]N-methylscopolamine$ ($[^{3}H]NMS$) showed that the dissociation constant ($K_d$) and the maximum binding value ($B_{max}$) were $3.3{\pm}0.8{\times}10^{10}$ M and $9.0{\pm}1.1$ fmol/mg protein, respectively. Binding competition experiments indicated that the affinities of C. elegans mAChRs to atropine, scopolamine, and oxotremorine were similar to those of mammalian mAChRs. Pirenzepine binding experiments revealed that the binding pattern of mAChRs in C. elegans closely resembled that of mAChRs in rat brain, suggesting that the receptors consist primarily of Ml subtype. The affinity of mAChRs for oxotrernorine was significantly affected by guanylylimidodiphosphate (Gpp(NH)p), a non hydrolyzable GTP analog, suggesting that mAChRs in C. elegans might be coupled to G proteins. The data presented here indicate the possibility that C. elegans provides a living animal model to study the action mode of the muscarinic cholinergic system.

• Biomolecules & Therapeutics
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• v.4 no.2
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• pp.196-201
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• 1996

The N-methyl-D-aspartate (NMDA) receptor-ion channel complex is activated by the simultaneous presence of L-glutamate and glycine, allowing the binding of MK-801 to the phencyclidine (PCP) site of the receptor. The $[^3H]$MK-801 binding assay system was established for determination of pharmacological functions of test compounds acting at the glycine site of the receptor. The binding in the presence of 0.1 $\mu$M L-glutamate was increased by an agonist (glycine) in a dose-dependent fashion, while decreased by either partial agonist (R-(+)-HA-966) or antagonist (5,7-dichlorokynurenic acid: 5,7-DCKA). To distinguish partial agonism from antagonism, various concentrations of 7-chlorokynurenic acid (7-CKA) were added in the assay to eliminate the interference of the endogenous glycine present in the membrane preparations. The bindings in the presence of L-glutamate (0.1$\muM$) and 7-CKA (1, 5, or 10$\muM$) were increased by R-(+)-HA-966. Being a weak partial agonist, the extent of potentiation was much less than that by the agonist. These binding profiles were clearly distinguishable from those by the antagonist, 5,7-DCKA, which exhibited no intrinsic activity. The binding assays established in the present study are a useful system to classify ligands acting at the glycine site of the NMDA receptor by their pharmacological functions.

• Journal of the Korean Magnetic Resonance Society
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• v.22 no.4
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• pp.125-131
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• 2018

Chemical shift perturbation (CSP) is a simple NMR technique for studying binding of a protein to various ligands. CSP is the only technique that can directly provide both a value for the dissociation constant and a binding site from the same set of measurements. To accurately analyze the CSP data, the exact binding mode such as multiple binding, should be carefully considered. In this review, we analyzed systematically the CSP data with multiple modes. This analysis might provide insight into the mechanism on how proteins selectively recognize their target ligands to achieve the biological function.

• Bulletin of the Korean Chemical Society
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• v.34 no.4
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• pp.1300-1302
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• 2013

• Archives of Pharmacal Research
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• v.7 no.2
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• pp.95-99
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• 1984

Binding of sulfaethidole to bovine serum albumin (BSA) was studied by circular dichroism. The effects of pH and ionic strength on the binding of sulfaethidole to BSA were investigated. It was found that one primary binding site on the BSAM was capable of inducing optical activity in the presence of sulfaethidole. Enhancement of the induced ellipticity of sulfaethidole upon addition to BSA was not much affected by the change of pH and ionic strength. Taking the effects of pH and ionic strength into consideration, it seems that the binding of sulfaethidole to BSA was not much affected by electrostatic and ionic interactions. Therefore, it might be assumed that the binding was mainly due to the hydrophobic interactions. Sulfaethidole seems to be a reasonable CD probe for the study of hydrophobic drug interactions.

• Journal of the Korean Magnetic Resonance Society
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• v.22 no.1
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• pp.18-25
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• 2018

Replication protein A (RPA) is an essential single-stranded DNA binding protein in DNA processing. It is known that N terminal domain of RPA70 (RPA70N) recruits various protein partners including damage-response proteins such as p53, ATRIP, Rad9, and MRE11. Although the common binding residues of RPA70N were revealed, dynamic properties of the protein are not studied yet. In this study, we measured $^{15}N$ relaxation parameters ($T_1,\;T_2$ and heteronuclear NOE) of human RPA70N and analyzed them using model-free analysis. Our data showed that the two loops near the binding site experience fast time scale motion while the binding site does not. It suggests that the protein binding surface of RPA70N is mostly rigid for minimizing entropy cost of binding and the loops can experience conformational changes.

• Proceedings of the Korean Institute of Building Construction Conference
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• 2016.05a
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• pp.51-52
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• 2016

This paper researches the Chloride Binding of Cement Paste according to the Ca/Si and Ca/Al Ratio. The mechanisms of chloride ion binding are not completely known, although it is believed that Alumina contents in cementitious system have an important role. For changing cement paste composition, Ordinary Portland Cement(OPC) paste is substituted by Granulated Ground Blast Slag(GGBS). With increasing the ratio of GGBS substitution(Thus alumina contents is increasing), The chloride binding capacity has a tendency to increase of binding chloride ion capacity.

• The Korean Journal of Physiology and Pharmacology
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• v.2 no.6
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• pp.671-676
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• 1998

In the present study, we first examined whether the changes in the DNA binding activities of the transcription factors, cAMP response element binding protein (CREB) and activator protein-1 (AP-1) mediate the long-term effects of morphine in differentiated SH-SY5Y human neuroblastoma cells. The increases in CREB and AP-1 DNA binding activities were time-dependent up to 6 days of morphine treatment (1, 4, and 6 days). However, the significant reduction in the DNA binding activities of CREB and AP-1 was observed after 10 days of chronic morphine $(10\;{\mu}M)$ administration. Secondly, we examined whether the changes of CREB and AP-1 DNA binding activities could be modulated by dopamine and haloperidol. Dopamine cotreatment moderately increased the levels of the CREB and AP-1 DNA binding activities induced by 10 days of chronic morphine treatment, and haloperidol cotreatment also resulted in a moderate increase of the CREB and AP-1 DNA binding activities. However, dopamine or haloperidol only treatment showed a significant increase or decrease of the CREB and AP-1 DNA binding activities, respectively. In the case of acute morphine treatment, the CREB and AP-1 DNA binding activities were shown to decrease in a time-dependent manner (30, 60, 90, and 120 min). Taken these together, in differentiated SH-SY5Y cells, morphine tolerance seems to involve simultaneous changes of the CREB and AP-1 DNA binding activities. Our data also suggest the possible involvement of haloperidol in prevention or reversal of morphine tolerance at the transcriptional level.