NMR structure and conformational dynamics of AtPDFL2.1, a defensin-like peptide from Arabidopsis thaliana

2016 ◽  
Vol 1864 (12) ◽  
pp. 1739-1747 ◽  
Author(s):  
Reza Omidvar ◽  
Youlin Xia ◽  
Fernando Porcelli ◽  
Holger Bohlmann ◽  
Gianluigi Veglia
Keyword(s):  
Arabidopsis Thaliana ◽  
Conformational Dynamics ◽  
Nmr Structure

NMR structure, conformational dynamics, and biological activity of Ps Def1 defensin from Pinus sylvestris

2017 ◽  
Vol 1865 (8) ◽  
pp. 1085-1094 ◽  
Author(s):  
Bulat I. Khairutdinov ◽  
Elena A. Ermakova ◽  
Yuri M. Yusypovych ◽  
Elena K. Bessolicina ◽  
Nadezhda B. Tarasova ◽  
...  
Keyword(s):  
Biological Activity ◽  
Pinus Sylvestris ◽  
Conformational Dynamics ◽  
Nmr Structure

NMR Structure of the Single QALGGH Zinc Finger Domain from the Arabidopsis thaliana SUPERMAN Protein

ChemBioChem ◽  
2003 ◽  
Vol 4 (2-3) ◽  
pp. 171-180 ◽  
Author(s):  
Carla Isernia ◽  
Enrico Bucci ◽  
Marilisa Leone ◽  
Laura Zaccaro ◽  
Paola Di Lello ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Zinc Finger ◽  
Nmr Structure ◽  
Zinc Finger Domain

Cover Picture: NMR Structure of the Single QALGGH Zinc Finger Domain from the Arabidopsis thaliana SUPERMAN Protein (ChemBioChem 2-3/2003)

ChemBioChem ◽  
2003 ◽  
Vol 4 (2-3) ◽  
pp. 125-125
Author(s):  
Carla Isernia ◽  
Enrico Bucci ◽  
Marilisa Leone ◽  
Laura Zaccaro ◽  
Paola Di Lello ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Zinc Finger ◽  
Nmr Structure ◽  
Zinc Finger Domain

scholarly journals NMR structure of CmPI-II, a non-classical Kazal protease inhibitor: Understanding its conformational dynamics and subtilisin A inhibition

2019 ◽  
Vol 206 (3) ◽  
pp. 280-294
Author(s):  
Aymara Cabrera-Muñoz ◽  
Pedro A. Valiente ◽  
Laritza Rojas ◽  
Maday Alonso-del-Rivero Antigua ◽  
José R. Pires
Keyword(s):  
Protease Inhibitor ◽  
Conformational Dynamics ◽  
Nmr Structure

scholarly journals AtTRB1–3 Mediates Structural Changes in AtPOT1b to Hold ssDNA

2014 ◽  
Vol 2014 ◽  
pp. 1-16 ◽  
Author(s):  
Amit Jaiswal
Keyword(s):  
Arabidopsis Thaliana ◽  
Molecular Docking ◽  
Structural Modification ◽  
Essential Role ◽  
Structural Changes ◽  
Conformational Dynamics ◽  
Genomic Stability ◽  
Telomeric Dna ◽  
Rich Region ◽  
Docking Interaction

POT from Arabidopsis thaliana is a member of shelterin complex and belongs to Telo_bind protein family. Three homologs are reported, namely, AtPOT1a, AtPOT1b, and AtPOT1c, where AtPOT1b is involved in genomic stability and chromosome end protection by providing necessary grip to G-rich region of telomeric DNA for telomerase assembly. Telomeric binding factors (TRB1–3) physically interact with POT with no known functionality. In this work attempt has been made to elucidate the reason behind the interaction by analyzing molecular docking interaction between AtPOT1b and AtTRB1–3, which yielded potential residues, which could play essential role in structural modification. 3 ns molecular simulation helped to look into structural stability and conformational dynamics portraying domain movements. AtTRB’s interaction with AtPOT1b provoked structural changes in AtPOT1b, thereby increasing the affinity for single strand DNA (ssDNA) as compared to double strand DNA (dsDNA). Although the obtained results require experimental evidence they can act as a guide in tracing the functions in other organisms. The information provided in this paper would be helpful in understanding functions of TRB1–3 with respect to genomic stability.

Stable genetic transformation of Arabidopsis thaliana by Agrobacterium inoculation in planta

1994 ◽  
Vol 5 (4) ◽  
pp. 551-558 ◽  
Author(s):  
Seok So Chang ◽  
Soon Ki Park ◽  
Byung Chul Kim ◽  
Bong Joong Kang ◽  
Dal Ung Kim ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Genetic Transformation ◽  
In Planta
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