The molecular basis of interaction domains of full-length PrP with lipid membranes

Nanoscale ◽  
2019 ◽  
Vol 11 (25) ◽  
pp. 12087-12091 ◽  
Author(s):  
Yangang Pan ◽  
Bin Wang ◽  
R. Alexander Reese ◽  
Bingqian Xu

A new method combining AFM measurements and molecular modeling was used to unravel the molecular basis of the interaction domains of full-length PrP with lipid membranes.

Biochemistry ◽  
2009 ◽  
Vol 48 (23) ◽  
pp. 5303-5312 ◽  
Author(s):  
Maoqing Dong ◽  
Polo C.-H. Lam ◽  
Delia I. Pinon ◽  
Ruben Abagyan ◽  
Laurence J. Miller

2006 ◽  
Vol 128 (43) ◽  
pp. 13982-13983 ◽  
Author(s):  
Rebecca Notman ◽  
Massimo Noro ◽  
Brendan O'Malley ◽  
Jamshed Anwar

2002 ◽  
Vol 74 (7) ◽  
pp. 1109-1116 ◽  
Author(s):  
M. Goodman ◽  
J. R. Del Valle ◽  
Y. Amino ◽  
E. Benedetti

In this presentation, we describe an integrated approach for the molecular basis for sweet taste among dipeptide-based ligands. By comparing the results obtained from X-ray diffraction studies with the conformations from NMR analysis and molecular modeling, we have observed recurring topochemical motifs that agree with previous models for sweet taste. In our examination of the unexplored D zone of the Tinti­Nofre model, we have uncovered a sweet potency enhancing effect of a new set of aralkyl-substitutions on dipeptide ligands, which reveals the importance of aromatic­aromatic interactions in maintaining high potency.


2000 ◽  
Vol 105 (2) ◽  
pp. 193-200 ◽  
Author(s):  
Jerome L Gabriel ◽  
Parkson Lee Gau Chong

1996 ◽  
Vol 4 (1) ◽  
pp. 35-38 ◽  
Author(s):  
Huipin Yuan ◽  
Angelica Leitmannova-Ottova ◽  
H.Ti Tien

2011 ◽  
Vol 1808 (11) ◽  
pp. 2685-2693 ◽  
Author(s):  
Annegret Boll ◽  
Aline Jatho ◽  
Nadine Czudnochowski ◽  
Matthias Geyer ◽  
Claudia Steinem
Keyword(s):  

2022 ◽  
Author(s):  
Clemence Claussin ◽  
Jacob Vazquez ◽  
Iestyn Whitehouse

Fundamental aspects of DNA replication, such as the anatomy of replication stall sites, how replisomes are influenced by gene transcription and whether the progression of sister replisomes is coordinated are poorly understood. Available techniques do not allow the precise mapping of the positions of individual replisomes on chromatin. We have developed a new method called Replicon-seq that entails the excision of full-length replicons by controlled nuclease cleavage at replication forks. Replicons are sequenced using Nanopore, which provides a single molecule readout of long DNA molecules. Using Replicon-seq, we have investigated replisome movement along chromatin. We found that sister replisomes progress with remarkable consistency from the origin of replication but function autonomously. Replication forks that encounter obstacles pause for a short duration but rapidly resume synthesis. The helicase Rrm3 plays a critical role both in mitigating the effect of protein barriers and facilitating efficient termination. Replicon-seq provides an unprecedented means of defining replisome movement across the genome.


2018 ◽  
Vol 150 (10) ◽  
pp. 1349-1349
Author(s):  
Caitlin Sedwick

New method predicts the molecular basis of membrane proteins’ voltage sensitivity.


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