CONFERENCE ON FRONTIERS OF NMR IN MOLECULAR BIOLOGY VII
CONFERENCE ON FRONTIERS OF NMR IN MOLECULAR BIOLOGY VII
批准号:
6225721
负责人:
STANLEY J OPELLA
金额:
$0.5万
依托单位:
依托单位国家:
美国
项目类别:
财政年份:
2001
资助国家:
美国
项目状态:
已结题
起止时间:
2001-03-05 至 2002-02-28
中文摘要
申请人的描述(Applicant's Description)
核磁共振(NMR)在生物医学中发挥着越来越重要的作用。
大分子结构的测定和蛋白质及
核酸动力学 核磁共振在结构生物学中的重要性与日俱增
生物学的新结构的数量有力地说明了
在过去的几年里,这项技术已经确定了大分子。 为
例如,大约250个新的NMR结构被沉积在PDB中,
一年,一个显着的数字,考虑到结构核磁共振场是
与成熟的结晶学领域相比仍处于发展阶段。
此外,越来越多的核磁共振组已建立在
大学、研究机构和工业界,反映了
领域 但核磁共振不仅是一种结构测定技术,
也能够提供丰富的信息,这是补充,
结构数据 蛋白质和核酸的动力学和溶剂化的NMR数据
酸变得可用,以及NMR表征部分
折叠或内折叠的蛋白质和多肽状态。 一个主要的研究目标是
以增加蛋白质或大分子复合物的大小,
通过NMR分析。 这就需要开发更高的领域
光谱仪,这将产生更高的灵敏度和更好的分辨率,
从而提高所有尺寸的结构的质量。 牵手小
这些工具的发展将是克服或
最小化相关时间问题。 尽管取得了重大进展,核磁共振数据
收藏仍然代表着在真实的时间和
设备的时间,并可能需要几个月的一个结构。 途径
通过高通量来寻求增加NMR结构的数量
方法或简化实验。 核磁共振是为数不多的
这将能够提供部分的结构和动力学数据,
折叠和异质蛋白质系统,即淀粉样蛋白。 研究这些
将对病理学和疾病产生重大影响。 会议将
该论坛介绍了重要蛋白质,核酸
酸及其复合物,阐明了关键的功能问题,
分子生物学 将进行方法和功能讨论
同等重量。 核磁共振的兴奋是生动地赞赏从核磁共振
《自然结构生物学》增刊,1998年7月5日,
《科学》上的新闻和观点文章,279,1127,1998
英文摘要
DESCRIPTION (Applicant's Description)
Nuclear Magnetic Resonance (NMR) is playing an increasingly important role in
the determination of macromolecular Structures and the study of protein and
nucleic acid dynamics. This growing importance of NMR in structural biology
is powerfully illustrated by the number of novel structures of biological
macromolecules determined by this technique over the last few years. For
example, approximately 250 new NMR structures are deposited in the PDB each
year, a remarkable number given the fact that the structural NMR field is
still in the developing phase compared to the mature area of crystallography.
In addition, a growing number of NMR groups have been established at
universities, research institutions, and industry, reflecting the vigor of the
field. But NMR is not only a technique for structure determination, it is
also able to provide a wealth of information which is complementary to the
structural data. NMR data on dynamics and solvation of proteins and nucleic
acids is becoming available as well as NMR characterization of partially
folded or infolded protein and polypeptide states. A major research goal is
to increase the size of the protein or macromolecular complex that can be
analyzed by NMR. This requires the development of even higher-field
spectrometers, which will yield higher sensitivity and better resolution,
thereby improving the quality of structures of all sizes. Hand in hand with
these instrument developments will be methodological approaches to overcome or
minimize the correlation time problem. Despite major advances, NMR data
collection still represents a substantial investment in real time and in
equipment time and may require several months for one structure. Avenues for
increasing the number of NMR Structures are sought through high throughput
approaches or streamlining experiments. NMR is one of very few techniques
which will be able to provide structural and dynamical data on partially
folded and heterogeneous protein systems, i.e. amyloids. Studies on these
will have major implications for pathology and disease. The meeting will be
the forum to present the newest structures of important proteins, nucleic
acids and complexes thereof, illuminating key functional questions in
molecular biology. Methodological and functional discussions will be given
equal weight. The excitement about NMR is vividly appreciated from the NMR
supplement of Nature Structural Biology, July 5, 1998 and a
News and Views article in Science, 279,1127,1998
期刊论文(0)
专著(0)
科研奖励(0)
会议论文
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