High-resolution13C NMR and multiple attenuated total internal reflectance IR spectroscopy of products of the interaction of HF with a cellulose anion exchanger

1989 ◽  
Vol 51 (4) ◽  
pp. 1080-1084
Author(s):  
R. G. Zhbankov ◽  
I. F. Alimov ◽  
T. A. Asaulova ◽  
A. A. �nnan ◽  
R. �. T��ya�r
1994 ◽  
Vol 64 (1) ◽  
pp. 91-95 ◽  
Author(s):  
Anuradha G. Rangamani ◽  
Peter T. McTigue ◽  
Bruce Verity

2005 ◽  
Vol 280 (23) ◽  
pp. 22245-22257 ◽  
Author(s):  
Marc L. Mendillo ◽  
Dan J. Mazur ◽  
Richard D. Kolodner

The Lac repressor-operator interaction was used as a reversible DNA end-blocking system in conjunction with an IAsys biosensor instrument (Thermo Affinity Sensors), which detects total internal reflectance and allows monitoring of binding and dissociation in real time, in order to develop a system for studying the ability of mismatch repair proteins to move along the DNA. The MSH2-MSH6 complex bound to a mispaired base was found to be converted by ATP binding to a form that showed rapid sliding along the DNA and dissociation via the DNA ends and also showed slow, direct dissociation from the DNA. In contrast, the MSH2-MSH6 complex bound to a base pair containing DNA only showed direct dissociation from the DNA. The MLH1-PMS1 complex formed both mispair-dependent and mispair-independent ternary complexes with the MSH2-MSH6 complex on DNA. The mispair-independent ternary complexes were formed most efficiently on DNA molecules with free ends under conditions where ATP hydrolysis did not occur, and only exhibited direct dissociation from the DNA. The mispair-dependent ternary complexes were formed in the highest yield on DNA molecules with blocked ends, required ATP and magnesium for formation, and showed both dissociation via the DNA ends and direct dissociation from the DNA.


CFW Plexus ◽  
2013 ◽  
Author(s):  
Frederick Warren ◽  
Cathrina Edwards ◽  
Benjamin Perston ◽  
Giusy Mandalari ◽  
Paul Royall ◽  
...  

2014 ◽  
Vol 9 (10) ◽  
pp. 2317-2328 ◽  
Author(s):  
Joshua Larson ◽  
Matt Kirk ◽  
Eric A Drier ◽  
William O'Brien ◽  
James F MacKay ◽  
...  

2004 ◽  
Vol 379 (3) ◽  
pp. 527-532 ◽  
Author(s):  
Richard M. EPAND ◽  
Phan VUONG ◽  
Christopher M. YIP ◽  
Shohei MAEKAWA ◽  
Raquel F. EPAND

A myristoylated peptide corresponding to the N-terminus of NAP-22 (neuronal axonal myristoylated membrane protein of 22 kDa) causes the quenching of the fluorescence of BODIPY®-TMR-labelled PtdIns(4,5)P2 in bilayers of 1-palmitoyl-2-oleoyl phosphatidylcholine containing 40 mol% cholesterol and 0.1 mol% BODIPY®–PtdIns(4,5)2. Both fluorescence spectroscopy and total internal reflectance fluorescence microscopy revealed the cholesterol-dependent nature of PtdIns(4,5)P2-enriched membrane-domain formation.


2006 ◽  
Vol 11 (3) ◽  
pp. 034011 ◽  
Author(s):  
Thomas Bruns ◽  
Wolfgang S. L. Strauss ◽  
Reinhard Sailer ◽  
Michael Wagner ◽  
Herbert Schneckenburger

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