BIOPHYSICAL CHARACTERIZATION OF ALPHA CRYSTALLIN
α 晶状体蛋白的生物物理特性
基本信息
- 批准号:6363131
- 负责人:
- 金额:$ 26.47万
- 依托单位:
- 依托单位国家:美国
- 项目类别:
- 财政年份:1994
- 资助国家:美国
- 起止时间:1994-06-01 至 2004-02-28
- 项目状态:已结题
- 来源:
- 关键词:
项目摘要
DESCRIPTION: Alpha-crystallin, tha major protein component of the
crystalline lens of mammalian eyes , exist in the lens cytoplasm as
aggregates of approximately 40 subunits in an isoform mixture of 3A:1B
in the human. Because of the way the lens develops throughout the
lifetime of an organism, a-crystallin and other lens proteins must (a)
be stable in structure and resistant to denaturation for a period of
years or decades; (b) must be present without superaggregation in
sufficient quantities to raise significantly the refractive index of the
lens; and (c) must be small and discrete enough to enable lens
transparency in the visible light spectrum. The recent discovery by
Horwitz that a-crystallin is related in sequence to the heat shock
protein family and that it can act in a chaperone-line fashion to
prevent the superaggregation of partially denatured proteins may explain
why it was "recruited" as a lens protein. It is present in all the
major non-lenticular tissues, but only in the lens are the two isoforms
of a-crystallin found together. The long-term objective of this
research is therefore to characterize the unique structural and
functional properties of a-crystallin that contribute to long-term
visual function and work against cataractogenesis. In the next grant
period, the specific aims are (a) to investigate comparatively the
structural and functional properties of native, reconstituted, and
renatured a-crystallin aggregates in order to characterize the basis for
their long-term stability; and (b) to compare the structural and
functional properties of the a -crystallin isoforms in order to
understand why it is only in the lens that both are found together. A
variety of biophysical and physical biochemical techniques will be
employed for this work, including circular dichroism spectropolarimetry
to study secondary structure, fast performance liquid chromatography,
fluorescence energy transfer, synchrotron scattering and diffraction,
electron microscopy, and rheometry.
描述:α -结晶蛋白,主要的蛋白质成分
项目成果
期刊论文数量(13)
专著数量(0)
科研奖励数量(0)
会议论文数量(0)
专利数量(0)
The role of the conserved COOH-terminal triad in alphaA-crystallin aggregation and functionality.
保守的 COOH 末端三联体在 αA-晶状体蛋白聚集和功能中的作用。
- DOI:
- 发表时间:2007
- 期刊:
- 影响因子:2.2
- 作者:Li,Ying;Schmitz,KarlR;Salerno,JohnC;Koretz,JaneF
- 通讯作者:Koretz,JaneF
Structural diversity in the small heat shock protein superfamily: control of aggregation by the N-terminal region.
小热休克蛋白超家族的结构多样性:N 末端区域对聚集的控制。
- DOI:10.1093/protein/gzg102
- 发表时间:2003
- 期刊:
- 影响因子:0
- 作者:Salerno,JohnC;Eifert,CherylL;Salerno,KathleenM;Koretz,JaneF
- 通讯作者:Koretz,JaneF
NH2-terminal stabilization of small heat shock protein structure: a comparison of two NH2-terminal deletion mutants of alphaA-crystallin.
小热休克蛋白结构的 NH2 末端稳定性:αA-晶状体蛋白的两种 NH2 末端缺失突变体的比较。
- DOI:
- 发表时间:2005
- 期刊:
- 影响因子:0
- 作者:Yang,Chaoxing;Salerno,JohnC;Koretz,JaneF
- 通讯作者:Koretz,JaneF
Analysis of the factors involved in the loss and restoration of the chaperone-like function of alpha-crystallin.
α-晶状体蛋白伴侣样功能丧失和恢复的相关因素分析。
- DOI:10.1006/bbrc.1997.6079
- 发表时间:1997
- 期刊:
- 影响因子:0
- 作者:Koretz,JF;Doss,EW;Reid,GH
- 通讯作者:Reid,GH
Heat-induced quaternary transitions in hetero- and homo-polymers of alpha-crystallin.
α-晶状体蛋白异聚物和均聚物中热诱导的四元转变。
- DOI:
- 发表时间:2001
- 期刊:
- 影响因子:0
- 作者:Burgio,MR;Bennett,PM;Koretz,JF
- 通讯作者:Koretz,JF
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Jane Koretz其他文献
Jane Koretz的其他文献
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{{ truncateString('Jane Koretz', 18)}}的其他基金
Multiscale Modeling of Accommodation and Presbyopia
调节和老花眼的多尺度建模
- 批准号:
7618167 - 财政年份:2008
- 资助金额:
$ 26.47万 - 项目类别:
Multiscale Modeling of Accommodation and Presbyopia
调节和老花眼的多尺度建模
- 批准号:
7485271 - 财政年份:2008
- 资助金额:
$ 26.47万 - 项目类别:
BIOPHYSICAL CHARACTERIZATION OF ALPHA-CRYSTALLIN
α-晶状体蛋白的生物物理特性
- 批准号:
2163710 - 财政年份:1994
- 资助金额:
$ 26.47万 - 项目类别:
BIOPHYSICAL CHARACTERIZATION OF ALPHA-CRYSTALLIN
α-晶状体蛋白的生物物理特性
- 批准号:
2163709 - 财政年份:1994
- 资助金额:
$ 26.47万 - 项目类别:
BIOPHYSICAL CHARACTERIZATION OF ALPHA CRYSTALLIN
α 晶状体蛋白的生物物理特性
- 批准号:
6164677 - 财政年份:1994
- 资助金额:
$ 26.47万 - 项目类别:
BIOPHYSICAL CHARACTERIZATION OF ALPHA CRYSTALLIN
α 晶状体蛋白的生物物理特性
- 批准号:
2630891 - 财政年份:1994
- 资助金额:
$ 26.47万 - 项目类别:
BIOPHYSICAL CHARACTERIZATION OF ALPHA-CRYSTALLIN
α-晶状体蛋白的生物物理特性
- 批准号:
2163711 - 财政年份:1994
- 资助金额:
$ 26.47万 - 项目类别:
BIOPHYSICAL CHARACTERIZATION OF ALPHA CRYSTALLIN
α 晶状体蛋白的生物物理特性
- 批准号:
2882904 - 财政年份:1994
- 资助金额:
$ 26.47万 - 项目类别:
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