Molecular Basis for the pH Dependent Structural Transition of Nitrophorin 4

2009 ◽  
Vol 113 (7) ◽  
pp. 2135-2142 ◽  
Author(s):  
Marcelo A. Martí ◽  
Dario A. Estrin ◽  
Adrián E. Roitberg
Keyword(s):  
Molecular Basis ◽  
Structural Transition ◽  
Nitrophorin 4 ◽  
Ph Dependent

scholarly journals A pH-dependent structural transition in the homopurine-homopyrimidine tract in superhelical DNA

1986 ◽  
Vol 2 (3) ◽  
pp. 115-124 ◽  
Author(s):  
V. I. Lyamichev ◽  
S. M. Mirkin ◽  
M. D. Frank-Kamenetskii
Keyword(s):  
Structural Transition ◽  
Ph Dependent

scholarly journals pH-Dependent Conformational Changes in Proteins and Their Effect on Experimental pKas: The Case of Nitrophorin 4

2012 ◽  
Vol 8 (11) ◽  
pp. e1002761 ◽  
Author(s):  
Natali V. Di Russo ◽  
Dario A. Estrin ◽  
Marcelo A. Martí ◽  
Adrian E. Roitberg
Keyword(s):  
Conformational Changes ◽  
Nitrophorin 4 ◽  
Ph Dependent

Determining the molecular basis for the pH-dependent interaction between 2′-deoxynucleotides and 9H-pyrido[3,4-b]indole in its ground and electronic excited states

2014 ◽  
Vol 16 (31) ◽  
pp. 16547-16562 ◽  
Author(s):  
M. Micaela Gonzalez ◽  
M. Paula Denofrio ◽  
Fernando S. García Einschlag ◽  
Carlos A. Franca ◽  
Reinaldo Pis Diez ◽  
...  
Keyword(s):  
Excited States ◽  
Molecular Basis ◽  
Electronic Excited States ◽  
Ph Dependent ◽  
Dependent Interaction

The nature of nucleotide and the pH modulate the type of complexes formed and the dynamic deactivation processes.

pH-dependent size and structural transition in P123 micelle induced gold nanoparticles

RSC Advances ◽  
2015 ◽  
Vol 5 (85) ◽  
pp. 69765-69775 ◽  
Author(s):  
P. Chatterjee ◽  
S. Hazra
Keyword(s):  
Gold Nanoparticles ◽  
Structural Transition ◽  
Ph Value ◽  
Ph Dependent

The transition of the structure and size of AuNPs at a pH value around 9.5, from slowly grown, well-faceted, large (≫19 nm), less uniform and near connected to fast grown, near symmetrical, small (<19 nm), more uniform and well-separated, is observed.

scholarly journals Molecular basis for pH-dependent mucosal dehydration in cystic fibrosis airways

2013 ◽  
Vol 110 (40) ◽  
pp. 15973-15978 ◽  
Author(s):  
A. L. Garland ◽  
W. G. Walton ◽  
R. D. Coakley ◽  
C. D. Tan ◽  
R. C. Gilmore ◽  
...  
Keyword(s):  
Cystic Fibrosis ◽  
Molecular Basis ◽  
Ph Dependent

scholarly journals pH-Dependent Picosecond Structural Dynamics in the Distal Pocket of Nitrophorin 4 Investigated by 2D IR Spectroscopy

2013 ◽  
Vol 117 (49) ◽  
pp. 15804-15811 ◽  
Author(s):  
Mark Cheng ◽  
Jennifer F. Brookes ◽  
William R. Montfort ◽  
Munira Khalil
Keyword(s):  
Ir Spectroscopy ◽  
Structural Dynamics ◽  
2D Ir ◽  
Nitrophorin 4 ◽  
Ph Dependent

scholarly journals A baton-relay mechanism for ER retrieval signal capture and proofreading by the KDEL receptor

2021 ◽  
Author(s):  
Andreas Gerondopoulos ◽  
Philipp Bräuer ◽  
Tomoaki Sobajima ◽  
Zhiyu Wu ◽  
Joanne L Parker ◽  
...  
Keyword(s):  
Molecular Basis ◽  
Carboxyl Terminus ◽  
Acidic Ph ◽  
Receptor Affinity ◽  
Neutral Ph ◽  
Binding Cavity ◽  
Arginine Residues ◽  
Ph Dependent ◽  
Kdel Receptor ◽  
Initial Capture

The KDEL-retrieval pathway captures escaped ER proteins with a KDEL or variant C-terminal signal at acidic pH in the Golgi and releases them at neutral pH in the ER. To address the mechanism of signal binding and the molecular basis for differences in signal affinity, we determined the HDEL and RDEL bound structures of the KDEL-receptor. Affinity differences are explained by interactions between the variable -4 position of the signal and W120, whereas initial capture of retrieval signals by their carboxyl-terminus is mediated by a baton-relay mechanism involving a series of conserved arginine residues in the receptor. This explains how the signal is first captured and then pulled into the binding cavity. During capture, retrieval signals undergo a selective proofreading step involving two gatekeeper residues D50 and E117 in the receptor. These mechanisms operate upstream of the pH-dependent closure of the receptor and explain the selectivity of the KDEL-retrieval pathway.

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