汤超
博士研究生 教授
北京大学 理论生物学中心,美国普林斯顿NEC研究所
生物物理方面
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- 姓名:汤超
- 目前身份:在职研究人员
- 担任导师情况:
- 学位:
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学术头衔:
博士生导师, 中国科学院院士
- 职称:高级-教授
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学科领域:
生物物理学
- 研究兴趣:生物物理方面
汤超,北京大学物理学院讲席教授,前沿交叉学科研究院执行院长。1977年考入中国科技大学力学系学习,1981年考取中美联合培养物理类研究生(CUSPEA)并赴美留学,1986年获美国芝加哥大学物理博士学位。先后在布鲁克海文国家实验室、加州大学圣巴巴拉分校理论物理研究所做博士后,1991年起在NEC美国普林斯顿研究所担任研究员、资深研究员,1997年被选为美国物理学会会士,2005年起在加州大学旧金山分校生物工程与治疗科学系、生物化学与生物物理系任终身正教授。2001年受李政道先生邀请,创立北京大学理论生物学中心。现任北京大学教授,前沿交叉学科研究院执行院长,定量生物学中心主任,北大-清华生命科学联合中心(北大)学术委员会主任。
主要从事系统生物学、定量生物学、物理生物学等领域的研究工作。多年来着力用物理学思想及方法研究生物问题,探索生命系统中的定量规律和设计原理。发表文章近百篇,被引用万余次。
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成果阅读
197
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成果数
5
【期刊论文】The yeast cell-cycle network is robustly designed
汤超, Fangting Li*†, Tao Long*†, Ying Lu*†, Qi Ouyang*‡, Chao Tang*‡§
PNAS April 6, 2004 vol. 101 no.14, 4781~4786,-0001,():
-1年11月30日
The interactions between proteins, DNA, and RNA in living cells constitute molecular networks that govern various cellular functions. To investigate the global dynamical properties and stabilities of such networks, we studied the cell-cycle regulatory network of the budding yeast. With the use of a simple dynamical model, it was demonstrated that the cell-cycle network is extremely stable and robust for its function. The biological stationary state, the G1 state, is a global attractor of the dynamics. The biological pathway, the cell-cycle sequence of protein states, is a globally attracting trajectory of the dynamics. These properties are largely preserved with respect to small perturbations to the network. These results suggest that cellular regulatory networks are robustly designed for their functions.
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【期刊论文】Self-Organized Criticality: An Explanation of l/f Noise
汤超, Per Bak, Chao Tang, Kurt Wiescnfeld
PHYSICAL REVIEW LETTERS, 1987, 59 (4): 381~384,-0001,():
-1年11月30日
We show that dynamical systems with spatial degrees of freedom naturally evolve into a self-organized critical point. Flicker noise, or l/f noise, can be identified with the dynamics of the critical state. This picture also yields insight into the origin of fractal objects.
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【期刊论文】Emergence of Preferred Structures in a Simple Model of Protein Folding
汤超, Hao Li, Robert Helling, *, Chao Tang, +, Ned Wingreen
Reprinr Series 2 August 1996, Volume 273, pp. 666-669,-0001,():
-1年11月30日
Protein structures in nature often exhibit a high degree of regularity (for examlple, secondary structure and tertiary symmetries) that is absent from random compact conformations. With the use of a simple lattice model of protein folding, it was demonstrated that structural regularities are related to high "designability" and evolutionary stability. The designability of each compact structure is measured by the number of sequences that can design the structure-that is, sequences that possess the structure as their nondegenerate ground state. Compact structures differ markedly in terms of their designability; highly designable. These highly designable structures possess "proteinlike", secondary structure and even tertiary symmetries. In addition, they are thermodynamically more stable than other structures. These results suggest that protein structures are selected in nature because they are readily designed and stable against mutations, and that such a selection simultaneously leads to thermodymamic stability.
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【期刊论文】Nature of Driving Force for Protein Folding: A Result From Analyzing the Statistical Potential
汤超, Hao Li, Chao Tang, Ned S. Wingreen
PHYS I CAL RE V I EW LETTERS, 1997, 79 (4): 765~768,-0001,():
-1年11月30日
In a statistical approach to protein structure analysis, Miyazawa and Jernigan derived a 20×20 matrix of inter-residue contact energies between different types of amino acids. Using the method of eigenvalue decomposition, we find that the Miyazawa-Jernigan matrix can be accurately reconstructed from its first two principal component vectors as Mij=C0+C1(qi+qj)+C2qiqj, with constant C's, and 20q values associated with the 20 amino acids. This regularity is due to hydrophobic interactions and a force of demixing, the latter obeying Hildebrand's solubility theory of simple liquids.
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【期刊论文】Are protein folds atypical?
汤超, HAO LI*, CHAO TANG†, AND NED S. WINGREEN
Proc. Natl. Acad. Sci. USA Vol. 95, pp. 4987-4990, April 1998,-0001,():
-1年11月30日
Protein structures are a very special class among all possible structures. It has been suggested that a "designability principle" plays a crucial role in nature's selection of protein sequences and structures. Here, we provide a theoretical base for such a selection principle, using a simple model of protein folding based on hydrophobic interactions. A structure is reduced to a string of 0s and 1s, which represent the surface and core sites, respectively, as the backbone is traced. Each structure is therefore associated with one point in a high dimensional space. Sequences are represented by strings of their hydrophobicities and thus can be mapped into the same space. A sequence that lies closer to a particular structure in this space than to any other structures will have that structure as its ground state. Atypical structures, namely those far away from other structures in the high dimensional space, have more sequences that fold into them and are thermodynamically more stable. We argue that the most common folds of proteins are the most atypical in the space of possible structures.
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