Theoretical investigation of the photoinitiated folding of HP-36.
Theoretical investigation of the photoinitiated folding of HP-36.
复制标题
HP-36光引发折叠的理论研究。
DOI：
10.1110/ps.062145106
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发表时间：
2006
期刊：
影响因子：
--
通讯作者：
Lin,ShengHsien
中科院分区：
文献类型：
--
作者：
Jang,Soonmin;Sreerama,Narasimha;Liao,VivianH-C;Lu,SHsiu-Feng;Li,Feng-Yin;Shin,Seokmin;Woody,RobertW;Lin,ShengHsien
A computational model was developed to examine the phototriggered folding of acagedprotein, a protein modified with an organic photolabile cross‐linker. Molecular dynamics simulations of the modified 36‐residue fragment of subdomain B of chicken villin head piece with a photolabile linker were performed, starting from both thecagedand theuncagedstructures. Construction of a free‐energy landscape, based on principal components as well as on radius of gyration versus root‐mean‐square deviation, and circular dichroism calculations were employed to characterize folding behavior and structures. The folded structures observed in the molecular dynamics trajectories were found to be similar to that of the wild‐type protein, in agreement with the published experimental results. The free‐energy landscapes of the modified and wild‐type proteins have similar topology, suggesting common thermodynamic/kinetic behavior. The existence of small differences in the free‐energy surface of the modified protein from that of the native protein, however, indicates subtle differences in the folding behavior.
