新抑癌素蛋白開散的熱力學與定量分析：生色團對蛋白穩定性的影響

賈琪華

3.237.71.247，Hello！

Close
Search Quick Search Advanced Search Publication Search	Personal Service Member Login Searching History Use Bonus Card SYMSKAN
Browse Browse by University of Graduate Thesis Browse by Pinyin of Graduate Thesis Browse by Conference Proceedings Topic Browse by Conference Proceedings Publisher Browse by Pinyin of Conference Proceedings Browse by eBook Category Browse by eBook Topic Browse by eBook Publisher
Customer Services Authorize Airiti Recommend a Journal

Search Symbol (Half-width)	Description of Search Symbols
Space	"AND" indicates the intertwining of key terms used in a search
Double Quotation Marks ("") ( " " )	Double quotation marks indicate the beginning and end of a phrase, and the search will only include terms that appear in the same order of those within the quotations. Example: "image process" ： " image process "
?	Indicates a variable letter. Entering two ? will indicate two variable letters, and so on. Example: "Appl?", search results will yield apple, apply… e , appl y … ( (often used to English word searches) )
*	Indicates an unlimited number of variable letters to follow, from 1~n. Example: Enter "appl*", search results will yield apple, apples, apply, applied, application…(often used in English word searches) e , appl es , appl y , appl ied , appl ication … ( (often used to English word searches) )
AND、OR、NOT	Boolean logic combinations of key words is a skill used to expand or refine search parameters. (1) AND (1) AND: Refines search parameters (2) OR (2) OR: Expands search parameters (3) NOT: Excludes irrelevant parameters

DOI stands for Digital Object Identifier （ D igital O bject I dentifier ） ,
and is the unique identifier for objects on the internet. It can be used to create persistent link and to cite articles.

Using DOI as a persistent link

To create a persistent link, add「http://dx.doi.org/」「 http://dx.doi.org/ 」 before a DOI.
For instance, if the DOI of an article is 10.5297/ser.1201.002 , you can link persistently to the article by entering the following link in your browser: http://dx.doi.org/ 10.5297/ser.1201.002 。
The DOI link will always direct you to the most updated article page no matter how the publisher changes the document's position, avoiding errors when engaging in important research.

Cite a document with DOI

When citing references, you should also cite the DOI if the article has one. If your citation guideline does not include DOIs, you may cite the DOI link.

DOIs allow accurate citations, improve academic contents connections, and allow users to gain better experience across different platforms. Currently, there are more than 70 million DOIs registered for academic contents. If you want to understand more about DOI, please visit airiti DOI Registration （ doi.airiti.com ）。

Data Source

Basic & Applied Sciences > Chemistry
College of Science > Department of Chemistry

Bibliography Management Tool

Related Links

Report an Issue

Search in Library

There is no full-text available at the moment. Airiti would like to request author's authorization. I would like to provide authorization.

新抑癌素蛋白開散的熱力學與定量分析：生色團對蛋白穩定性的影響

Thermodynamic and Quantitative Analysis of Unfolding of apo- and holoNeocarzinostatin: Effect of Labile Chromophore on Protein Stability

賈琪華 , Ph.D　　Advisor：金德航　　Co-advisor ：陸大榮

英文

新抑癌素；蛋白開散；熱力學與定量分析； Neocarzinostatin ； Unfolding ； Thermodynamic and Quantitative Analysis

Abstract │ Reference (164) │ Altmetrics

Abstract 〈TOP〉

Parallel Abstract 〈TOP〉

Neocarzinostatin, the first enediyne antitumor antibiotic chromoprotein, consists of an all β-sheet protein and a biologically active chromophore. We investigated the protein stability against thermal unfolding in the pH range of 2–10 with and without urea. At room temperature, the apoprotein is stable at pH between 4 and 10, whereas the stability decreases below pH 4. By two-dimensional unfolding studies, the ∆H and ∆Cp of the protein were estimated to be 65±1 kcal/mol and 1.04±0.03 kcal/mol/K, respectively. Conformational changes followed by the near-UV circular dichroism show the disrupted tertiary structure at low temperatures in aponeocarzinostatin but not in its holo form. The results suggest that labile chromophore is able to protect the carrier protein against cold denaturation. We therefore systematically examined differential protein stability between apo and holo form under versatile conditions. The protein stability correlates well with the presence of protein-bound chromophore. The protein in holo form is more stable than its apo form under acidic conditions, where the chromophore is relatively stable. As a result of this finding, we further examined thermal unfolding of aponeocarzinostatin under acidic conditions and observed an intermediate with residual structure at pH 2.0 and 324 K.

Reference ( 164 ) 〈TOP〉

Abe, S., and Otsuki, M. (2002) Styrene maleic acid neocarzinostatin treatment for hepatocellular carcinoma. Curr Med Chem Anticancer Agents 2, 715-26.
連結：
Adjadj, E., Mispelter, J., Quiniou, E., Dimicoli, J. L., Favaudon, V., and Lhoste, J. M. (1990) Proton NMR studies of apo-neocarzinostatin from Streptomyces carzinostaticus. Sequence-specific assignment and secondary structure. Eur J Biochem 190, 263-71.
連結：
Adjadj, E., Quiniou, E., Mispelter, J., Favaudon, V., and Lhoste, J. M. (1992) The seven-stranded beta-barrel structure of apo-neocarzinostatin as compared to the immunoglobulin domain. Biochimie 74, 853-8.
連結：
Adjadj, E., Quiniou, E., Mispelter, J., Favaudon, V., and Lhoste, J. M. (1992) Three-dimensional solution structure of apo-neocarzinostatin from Streptomyces carzinostaticus determined by NMR spectroscopy. Eur J Biochem 203, 505-11.
連結：
Albers-Schonberg, G., Dewey, R. S., Hensens, O. D., Liesch, J. M., Napier, M. A., and Goldberg, I. H. (1980) Neocarzinostatin: chemical characterization and partial structure of the non-protein chromophore. Biochem Biophys Res Commun 95, 1351-6.
連結：

Altmetrics

〈TOP〉

E-mail ：

When an article is available to download, a notice will be sent to your mailbox address.

E-mail ：