Influence of local and residual structures on the scaling behavior and dimensions of unfolded proteins
文献类型：期刊论文
| 作者 | Wang, Zhisong; Plaxco, Kevin W.; Makarov, Dmitrii E. |
| 刊名 | BIOPOLYMERS
 |
| 出版日期 | 2007-07-01 |
| 卷号 | 86页码:321-328 |
| 关键词 | unfolded proteins random coil alpha-helix PPII helix Monte Carlo simulation |
| ISSN号 | 0006-3525 |
| DOI | 10.1002/bip.20747 |
| 英文摘要 | Although recent spectroscopic studies of chemically denatured proteins hint at significant nonrandom residual structure, the results of extensive small angle X-ray scattering studies suggest random coil behavior, calling for a coherent understanding of these seemingly contradicting observations. Here, we report the results of a Monte Carlo study of the effects of two types of local structures, a helix and Polyproline II(PPII) helix, on the dimensions of random coil polyalanine chains viewed as a model of highly denatured proteins. We find that although Flory's power law scaling, long regarded as a signature of random coil behavior, holds for chains containing up to 90% a or PPII helix, the absolute magnitude of the chain dimensions is sensitive to helix content. As residual alpha helix content increases, the chain contracts until it reaches a minimum radius at similar to 70% helix, after which the chain dimensions expand rapidly. With an a helix content of similar to 20%, corresponding to the Ramachandran probability of being in the helical basin, experimentally observed radii of gyration are recovered. Experimental radii are similarly recovered at an a helix content of similar to 87%, providing an explanation for the previously puzzling experimental finding that the dimensions of the highly helical methanol-induced unfolded state are experimentally indistinguishable from those of the helix-poor urea-unfolded state. In contrast, the radius of gyration increases monotonically with increasing PPII content, and is always more expanded than the dimensions observed experimentally. These results suggest that PPII is unlikely the sole, dominant preferred conformation for unfolded proteins. (c) 2007 Wiley Periodicals, Inc. |
| WOS关键词 | POLYPROLINE-II STRUCTURE ; DENATURED PROTEIN ; RANDOM-COIL ; SCATTERING FUNCTION ; POLYPEPTIDE-CHAINS ; STATE ; HELIX ; UREA ; CONFORMATION ; PEPTIDES |
| WOS研究方向 | Biochemistry & Molecular Biology ; Biophysics |
| 语种 | 英语 |
| WOS记录号 | WOS:000247575600008 |
| 出版者 | JOHN WILEY & SONS INC |
| 源URL | [http://119.78.100.186/handle/113462/27330]  |
| 专题 | 中国科学院近代物理研究所 |
| 通讯作者 | Wang, Zhisong |
| 作者单位 | 1.Fudan Univ, Inst Modern Phys, Appl Ion Beam Phys Lab, Shanghai 200433, Peoples R China 2.Univ Texas, Dept Chem & Biochem, Inst Theoret Chem, Austin, TX 78712 USA 3.Univ Calif Santa Barbara, Dept Chem & Biochem, Santa Barbara, CA 93106 USA |
| 推荐引用方式 GB/T 7714 | Wang, Zhisong,Plaxco, Kevin W.,Makarov, Dmitrii E.. Influence of local and residual structures on the scaling behavior and dimensions of unfolded proteins[J]. BIOPOLYMERS,2007,86:321-328. |
| APA | Wang, Zhisong,Plaxco, Kevin W.,&Makarov, Dmitrii E..(2007).Influence of local and residual structures on the scaling behavior and dimensions of unfolded proteins.BIOPOLYMERS,86,321-328. |
| MLA | Wang, Zhisong,et al."Influence of local and residual structures on the scaling behavior and dimensions of unfolded proteins".BIOPOLYMERS 86(2007):321-328. |
入库方式： OAI收割
来源：近代物理研究所
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