Jiangguo Lin¹, Botao Xiao^1,2, Quhuan Li¹, Ying Fang¹, Jianhua Wu^1,*

Molecular & Cellular Biomechanics, Vol.15, No.1, pp. 37-49, 2018, DOI:10.3970/mcb.2018.015.037

Abstract The protein structure-function paradigm implies that the structure of a protein defines its function. Crystallization techniques such as X-ray, electron microscopy (EM) and nuclear magnetic resonance (NMR) have been applied to resolve the crystal structure of numerous proteins, provided beautiful and informative models of proteins. However, proteins are not intrinsically in static state but in dynamic state, which is lack in crystal models. The protein flexibility, a key mechanical property of proteins, plays important roles in various biological processes, such as ligand-receptor interaction, signaling transduction, substrate recognition and post-translational modifications. Advanced time-resolved crystallography has been developed recent years to visualize… More >

Q.W.Yang¹, J.K.Liu², C.H. Li³

CMES-Computer Modeling in Engineering & Sciences, Vol.91, No.4, pp. 313-335, 2013, DOI:10.3970/cmes.2013.091.313

Abstract A method based on best achievable flexibility change is presented in this paper to localize and quantify multiple damages in structures. The key process of the damage localization approach is the computation of the Euclidean distances between the measured flexibility change and the best achievable flexibility changes. The location of damage can be identified by searching for a value that is considerably smaller than others in these distances. For the multiple-damage case, a sequential damage localization approach is proposed to locate the damage sites one by one. With the suspected damaged elements determined, the flexibility sensitivity method is employed to… More >