Characterization of local polarity and hydrophobic binding sites of beta-lactoglobulin by using N-terminal specific fluorescence labeling
文献类型：期刊论文
| 作者 | Dong, SY; Zhao, ZW; Ma, HM |
| 刊名 | JOURNAL OF PROTEOME RESEARCH
 |
| 出版日期 | 2006 |
| 卷号 | 5期号:1页码:26-31 |
| 关键词 | Characterization Of Hydrophobic Binding Sites Local Polarity Detection N-terminal Specific Labeling Beta-lactoglobulin |
| ISSN号 | 1535-3893 |
| DOI | 10.1021/pr0501968 |
| 英文摘要 | Because of wide ligand-binding ability and significant industrial interest of beta-lactoglobulin (beta-LG), its binding properties have been extensively studied. However, there still exists a controversy as to where a ligand binds, since at least two potential hydrophobic binding sites in beta-LG have been postulated for ligand binding: an internal one (calyx) and an external one (near the N-terminus). In this work, the local polarity and hydrophobic binding sites of beta-LG have been characterized by using N-terminal specific fluorescence labeling combined with a polarity-sensitive fluorescent probe 3-(4-chloro-6-hydrazino- 1,3,5-triazinylamino)-7-(dimethylamino)-2-methylphenazine (CHTDP). The polarity within the calyx is found to be extremely low, which is explained in terms of superhydrophobicity possibly resulting from its nanostructure, and the polarity is increased with the destruction of the calyx by heat treatment. However, the polarity of the N-terminal domain in native beta-LG is decreased after thermal denaturation. This polarity trend toward decreasing instead of increasing shows that beta-LG may have no definite external hydrophobic binding site. The hydrophobic binding of a ligand such as CHTDP at the surface of the protein is probably achieved via appropriate assembling of corresponding hydrophobic residues rather than via a fixed external hydrophobic binding site. Also, the ligand-binding location in beta-LG is found to be relevant to not only experimental conditions (pH <= 6.2 or pH > 7.1) but also binding mechanisms (hydrophobic affinity or electrostatic interaction). |
| 语种 | 英语 |
| WOS记录号 | WOS:000234668300002 |
| 出版者 | AMER CHEMICAL SOC |
| 源URL | [http://ir.iccas.ac.cn/handle/121111/57927]  |
| 专题 | 中国科学院化学研究所 |
| 通讯作者 | Ma, HM |
| 作者单位 | Chinese Acad Sci, Inst Chem, Ctr Mol Sci, Beijing 100080, Peoples R China |
| 推荐引用方式 GB/T 7714 | Dong, SY,Zhao, ZW,Ma, HM. Characterization of local polarity and hydrophobic binding sites of beta-lactoglobulin by using N-terminal specific fluorescence labeling[J]. JOURNAL OF PROTEOME RESEARCH,2006,5(1):26-31. |
| APA | Dong, SY,Zhao, ZW,&Ma, HM.(2006).Characterization of local polarity and hydrophobic binding sites of beta-lactoglobulin by using N-terminal specific fluorescence labeling.JOURNAL OF PROTEOME RESEARCH,5(1),26-31. |
| MLA | Dong, SY,et al."Characterization of local polarity and hydrophobic binding sites of beta-lactoglobulin by using N-terminal specific fluorescence labeling".JOURNAL OF PROTEOME RESEARCH 5.1(2006):26-31. |
入库方式： OAI收割
来源：化学研究所
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