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Thermodynamics of nucleotide binding to the chaperonin GroEL studied by isothermal titration calorimetry: Evidence for noncooperative nucleotide binding.
https://ir.soken.ac.jp/records/4286
https://ir.soken.ac.jp/records/428618ca1840-a4c7-4982-8fc1-5ea86ce7f83d
| Item type | 学術雑誌論文 / Journal Article(1) | |||||||||
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| 公開日 | 2014-03-12 | |||||||||
| タイトル | ||||||||||
| タイトル | Thermodynamics of nucleotide binding to the chaperonin GroEL studied by isothermal titration calorimetry: Evidence for noncooperative nucleotide binding. | |||||||||
| タイトル | ||||||||||
| タイトル | Thermodynamics of nucleotide binding to the chaperonin GroEL studied by isothermal titration calorimetry: Evidence for noncooperative nucleotide binding. | |||||||||
| 言語 | en | |||||||||
| 言語 | ||||||||||
| 言語 | eng | |||||||||
| 資源タイプ | ||||||||||
| 資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||||||
| 資源タイプ | journal article | |||||||||
| アクセス権 | ||||||||||
| アクセス権 | metadata only access | |||||||||
| アクセス権URI | http://purl.org/coar/access_right/c_14cb | |||||||||
| 著者 |
TERADA, Tomoki P
× TERADA, Tomoki P
× KUWAJIMA, Kunihiro
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| 著者別名 |
桑島, 邦博
× 桑島, 邦博
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| 抄録 | ||||||||||
| 内容記述タイプ | Abstract | |||||||||
| 内容記述 | We characterized the thermodynamics of binding reactions of nucleotides ADP and ATPγS (a nonhydrolyzable analog of ATP) to GroEL in a temperature range of 5°C to 35°C by isothermal titration calorimetry. Analysis with a noncooperative binding model has shown that the bindings of nucleotides are driven enthalpically with binding constants of 7×103 M−1 and 4×104 M−1 for ADP and ATPγS, respectively, at 26°C and that the heat capacity change ΔCp is about 100 cal/mol⋅K for both the nucleotides. The stoichiometries of binding were about 8 and 9 molecules for ADP and ATPγS, respectively, per GroEL tetradecamer at 5°C, and both increased with temperature to reach about 14 (ADP) and 12 (ATPγS) for both nucleotides at 35°C. The absence of initial increase of binding heat as well as Hill coefficient less than 1.2, which were obtained from the fitting to the model curve by assuming positive cooperativity, showed that there was virtually no positive cooperativity in the nucleotide bindings. Incorporating a difference in affinity for the nucleotide (ADP and ATPγS) between the two rings of GroEL into the noncooperative binding model improved the goodness of fitting and the difference in the affinity increased with decreasing temperature. | |||||||||
| 書誌情報 |
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology en : Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 巻 1431, 号 2, p. 269-281, 発行日 1999-05-18 |
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| 出版者 | ||||||||||
| 出版者 | Elsevier | |||||||||
| ISSN | ||||||||||
| 収録物識別子タイプ | ISSN | |||||||||
| 収録物識別子 | 0006-3002 | |||||||||
| 権利 | ||||||||||
| 権利情報 | © 1999 Elsevier Science B.V. | |||||||||
