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Conformational Ensembles from Experimental Data
and Computer Simulations
Poster Abstracts
141
104-POS
Board 24
The Connections Between Coherent Fluctuations and Native Structures af Proteins
Wang Jun
1,2,3
, Qian-Yuan Tang
1
, Wei Wang
1,2,3
.
1
Nanjing University, Nanjing, Jiangsu, China,
2
National Lab of Solid State Microstructure,
Nanjing, Jiangsu, China,
3
Collaborative Innovation Center of Advanced Microstructures,
Nanjing, Jiangsu, China.
Recently, it is observed that the structural fluctuations of globular proteins exhibit long-range
correlations which resemble the behavior around critical point. This kind of dynamic behaviors
are universal for all globular proteins. What are the physical sources of such kind of behaviors?
Are there sequential or structural signatures for this kind of dynamic behaviors? The connections
between structure (sequence) and the fluctuation dynamics may help to understand the
characteristics and evolution of natural proteins. In present work, the coherent fluctuations and
the features of landscapes are connected based on a physical consideration. To exemplify this
kind of connection, the fluctuations of proteins are analyzed with elastic network models. It is
found that the proteins also exhibit highly correlated fluctuations starting from only the native
conformations determined through X-ray diffraction. The scale-free behavior is also true for the
B-factor in X-ray experiment. This clearly demonstrates the connection between coherent
fluctuation and the features of vibrational spectrums of proteins. Some structural analysis
demonstrate that the coherent fluctuations may comes from some special features of structure
and interactions. These results are consistent with previous simulations and bioinformatics
studies, and may help to understand the design principle of natural proteins.