Solid-State and Solution NMR Studies of the CAP-Gly Domain of Mammalian Dynactin and Its Interaction with Microtubules

2009 ◽  
Vol 131 (29) ◽  
pp. 10113-10126 ◽  
Author(s):  
Shangjin Sun ◽  
Amanda Siglin ◽  
John C. Williams ◽  
Tatyana Polenova
Keyword(s):  
2010 ◽  
Vol 114 (48) ◽  
pp. 15991-16002 ◽  
Author(s):  
Prashant S. Emani ◽  
Gregory L. Olsen ◽  
Dorothy C. Echodu ◽  
Gabriele Varani ◽  
Gary P. Drobny

2016 ◽  
Vol 40 (8) ◽  
pp. 7181-7189 ◽  
Author(s):  
Martin J. D. Champion ◽  
William Levason ◽  
David Pugh ◽  
Gillian Reid

The hydrogen bonding of hexahalometallate anions with various organic cations is explored via crystallographic and solution NMR studies.


ChemInform ◽  
1990 ◽  
Vol 21 (37) ◽  
Author(s):  
T. BERINGHELLI ◽  
G. D'ALFONSO ◽  
G. CIANI ◽  
A. SIRONI ◽  
H. MOLINARI

2004 ◽  
Vol 279 (44) ◽  
pp. 45815-45823 ◽  
Author(s):  
Fernando Porcelli ◽  
Bethany Buck ◽  
Dong-Kuk Lee ◽  
Kevin J. Hallock ◽  
Ayyalusamy Ramamoorthy ◽  
...  

Pardaxins are a class of ichthyotoxic peptides isolated from fish mucous glands. Pardaxins physically interact with cell membranes by forming pores or voltage-gated ion channels that disrupt cellular functions. Here we report the high-resolution structure of synthetic pardaxin Pa4 in sodium dodecylphosphocholine micelles, as determined by1H solution NMR spectroscopy. The peptide adopts a bend-helix-bend-helix motif with an angle between the two structure helices of 122 ± 9°, making this structure substantially different from the one previously determined in organic solvents. In addition, paramagnetic solution NMR experiments on Pa4 in micelles reveal that except for the C terminus, the peptide is not solvent-exposed. These results are complemented by solid-state NMR experiments on Pa4 in lipid bilayers. In particular,13C-15N rotational echo double-resonance experiments in multilamellar vesicles support the helical conformation of the C-terminal segment, whereas2H NMR experiments show that the peptide induces considerable disorder in both the head-groups and the hydrophobic core of the bilayers. These solid-state NMR studies indicate that the C-terminal helix has a transmembrane orientation in DMPC bilayers, whereas in POPC bilayers, this domain is heterogeneously oriented on the lipid surface and undergoes slow motion on the NMR time scale. These new data help explain how the non-covalent interactions of Pa4 with lipid membranes induce a stable secondary structure and provide an atomic view of the membrane insertion process of Pa4.


2006 ◽  
Vol 691 (5) ◽  
pp. 869-878 ◽  
Author(s):  
Krystyna Kurdziel ◽  
Sebastian Olejniczak ◽  
Andrzej Okruszek ◽  
Tadeusz Głowiak ◽  
Rafał Kruszyński ◽  
...  

2007 ◽  
Vol 37 (4) ◽  
pp. 303-312 ◽  
Author(s):  
Karla Werner ◽  
Ines Lehner ◽  
Harpreet Kaur Dhiman ◽  
Christian Richter ◽  
Clemens Glaubitz ◽  
...  

2007 ◽  
Vol 21 (1) ◽  
pp. 61-67 ◽  
Author(s):  
Norah O. Al-Zamil ◽  
Khulood A. Al-Sadhan ◽  
Anvarhusein A. Isab ◽  
Mohamed I.M. Wazeer ◽  
Abdul Rehman A. Al-Arfaj

Mixed ligand complexes of Ag(I) with triphenylphosphine (PPh3), triphenylphosphine sulfide (SPPh3), triphenylphosphine selenide (SePPh3) and Imidazolidine-2-thione (Imt) have been prepared. The solution as well as solid state NMR studies have been carried out to characterize these complexes. Both solid and solution NMR show the coordination via thione group on one side and (S/Se) or PPh3on the other side. A higher antimicrobial activity is shown by [ImtAgPPh3]Cl complex against gram negativePseudomonas aeruginosa(P. aeruginosa) andEscherichia coli(E. coli) compared to the other two complexes i.e. [ImtAgSPPh3]Cl and [ImtAgSePPh3]Cl.


Author(s):  
David C. Apperley ◽  
William Clegg ◽  
Simon Coles ◽  
Joanne L. Coyle ◽  
Noreen Martin ◽  
...  
Keyword(s):  

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