Molecular Insight into the β-Sheet Twist and Related Morphology of Self-Assembled Peptide Amphiphile Ribbons

Author(s):  
Qinsi Xiong ◽  
Samuel I. Stupp ◽  
George C. Schatz
Open Biology ◽  
2013 ◽  
Vol 3 (11) ◽  
pp. 130100 ◽  
Author(s):  
Zhisheng Lu ◽  
Julien R. C. Bergeron ◽  
R. Andrew Atkinson ◽  
Torsten Schaller ◽  
Dennis A. Veselkov ◽  
...  

The HIV-1 viral infectivity factor (Vif) neutralizes cell-encoded antiviral APOBEC3 proteins by recruiting a cellular ElonginB (EloB)/ElonginC (EloC)/Cullin5-containing ubiquitin ligase complex, resulting in APOBEC3 ubiquitination and proteolysis. The suppressors-of-cytokine-signalling-like domain (SOCS-box) of HIV-1 Vif is essential for E3 ligase engagement, and contains a BC box as well as an unusual proline-rich motif. Here, we report the NMR solution structure of the Vif SOCS–ElonginBC (EloBC) complex. In contrast to SOCS-boxes described in other proteins, the HIV-1 Vif SOCS-box contains only one α-helical domain followed by a β-sheet fold. The SOCS-box of Vif binds primarily to EloC by hydrophobic interactions. The functionally essential proline-rich motif mediates a direct but weak interaction with residues 101–104 of EloB, inducing a conformational change from an unstructured state to a structured state. The structure of the complex and biophysical studies provide detailed insight into the function of Vif's proline-rich motif and reveal novel dynamic information on the Vif–EloBC interaction.


2014 ◽  
Vol 43 (29) ◽  
pp. 11277-11285 ◽  
Author(s):  
Bernhard Breit ◽  
Urs Gellrich ◽  
Timothy Li ◽  
Jason M. Lynam ◽  
Lucy M. Milner ◽  
...  

A combined computational and experimental study into the mechanism of the anti-Markovnikov hydration of phenylacetylene by a self-assembled ligand complex.


Structure ◽  
2010 ◽  
Vol 18 (1) ◽  
pp. 138-147 ◽  
Author(s):  
Eri Sakata ◽  
Tadashi Satoh ◽  
Shunsuke Yamamoto ◽  
Yoshiki Yamaguchi ◽  
Maho Yagi-Utsumi ◽  
...  

2012 ◽  
Vol 2012 ◽  
pp. 1-5 ◽  
Author(s):  
Leila Costelle ◽  
Liina Lind ◽  
Pasi Jalkanen ◽  
Minna T. Räisänen ◽  
Roman Nowak ◽  
...  

Self-assembled monolayers (SAMs) are promising materials for micromechanical applications. However, characterization of mechanical properties of monolayers is challenging for standard nanoindentation, and new efficient analysis techniques are needed. Hereby, a conventional nanoindentation method has been combined in a unique way with efficient data analysis based on consumed energy calculation and load-displacement data. The procedure has been applied on SAMs of 4,4′-biphenyldithiol (BPDT) on Au, 1-tetradecanethiol (TDT), and 1-hexadecanethiol (HDT) on Au and Ag substrates being the first study where SAMs of the same thiols on different substrates are analyzed by nanoindentation providing a new insight into the substrate effects. Unlike TDT and HDT SAMs, which are found to strongly enhance the homogeneity and stiffness of the underlying substrate, the BPDT covered Au substrate appears softer in mechanical response. In the case of TDT and HDT SAMs on Ag the structures are softer showing also faster relaxation than the corresponding structures on Au substrate. The proposed procedure enables a fast and efficient way of assessing the complex behaviour of SAM modified substrates. As a consequence, the results are relevant to practical issues dependent on layer activity and toughness.


2010 ◽  
Vol 122 (13) ◽  
pp. 2404-2407 ◽  
Author(s):  
Atalia Birman ◽  
Kristian Kjaer ◽  
Yehiam Prior ◽  
Iftach Nevo ◽  
Leslie Leiserowitz

2018 ◽  
Vol 130 (26) ◽  
pp. 7835-7839 ◽  
Author(s):  
David E. Clarke ◽  
Christopher D. J. Parmenter ◽  
Oren A. Scherman
Keyword(s):  

2018 ◽  
Vol 57 (26) ◽  
pp. 7709-7713 ◽  
Author(s):  
David E. Clarke ◽  
Christopher D. J. Parmenter ◽  
Oren A. Scherman
Keyword(s):  

2020 ◽  
Vol 11 (28) ◽  
pp. 4547-4556
Author(s):  
Hayeon Kim ◽  
Inhye Kim ◽  
Jun Ho Hwang ◽  
Jaehyun Park ◽  
Hyungju Ahn ◽  
...  

The drug loading/releasing capability of GSH-responsive nanovesicles self-assembled from peptide amphiphiles was controlled by varying the location and number of disulfide-linkages in the peptide for the selective drug-release into tumor cells.


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