排序方式: 共有76条查询结果,搜索用时 15 毫秒
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Andreas Maaßen Dr. Jan M. Gebauer Elena Theres Abraham Isabelle Grimm Dr. Jörg-Martin Neudörfl Dr. Ronald Kühne Prof. Dr. Ines Neundorf Prof. Dr. Ulrich Baumann Prof. Dr. Hans-Günther Schmalz 《Angewandte Chemie (Weinheim an der Bergstrasse, Germany)》2020,132(14):5796-5804
Collagen model peptides (CMPs) serve as tools for understanding stability and function of the collagen triple helix and have a potential for biomedical applications. In the past, interstrand cross-linking or conformational preconditioning of proline units through stereoelectronic effects have been utilized in the design of stabilized CMPs. To further study the effects determining collagen triple helix stability we investigated a series of CMPs containing synthetic diproline-mimicking modules (ProMs), which were preorganized in a PPII-helix-type conformation by a functionalizable intrastrand C2 bridge. Results of CD-based denaturation studies were correlated with calculated (DFT) conformational preferences of the ProM units, revealing that the relative helix stability is mainly governed by an interplay of main-chain preorganization, ring-flip preference, adaptability, and steric effects. Triple helix integrity was proven by crystal structure analysis and binding to HSP47. 相似文献
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《Chemie in Unserer Zeit》2017,51(1):26-33
The interior of a living cell is very distinct from dilute aqueous solutions that are often used to study the function of proteins and enzymes experimentally. Here, we discuss novel experimental techniques and modeling approaches that provide a deeper understanding of the effects of crowding, intermolecular interactions, and the influence of osmolytes in realistic biological environments, including cells. Further, we discuss adaptation mechanisms involving in‐cell solvation environments to extreme conditions, such as high pressure in the deep sea, and their relevance to biotechnology. 相似文献
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《Angewandte Chemie (Weinheim an der Bergstrasse, Germany)》2017,129(25):7176-7179
The kinase inhibitory domain of the cell cycle regulatory protein p27Kip1 (p27) was nuclear spin hyperpolarized using dissolution dynamic nuclear polarization (D‐DNP). While intrinsically disordered in isolation, p27 adopts secondary structural motifs, including an α‐helical structure, upon binding to cyclin‐dependent kinase 2 (Cdk2)/cyclin A. The sensitivity gains obtained with hyperpolarization enable the real‐time observation of 13C NMR signals during p27 folding upon binding to Cdk2/cyclin A on a time scale of several seconds. Time‐dependent intensity changes are dependent on the extent of folding and binding, as manifested in differential spin relaxation. The analysis of signal decay rates suggests the existence of a partially folded p27 intermediate during the timescale of the D‐DNP NMR experiment. 相似文献
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