Solution structure and dynamics of lanthanide(III) complexes of diethylenetriaminepentaacetate: a two-dimensional NMR analysis

1988 ◽  
Vol 27 (26) ◽  
pp. 4730-4738 ◽  
Author(s):  
Bruce G. Jenkins ◽  
Randall B. Lauffer
Keyword(s):  
Solution Structure ◽  
Two Dimensional ◽  
Nmr Analysis ◽  
Structure And Dynamics

scholarly journals Understanding the structure and dynamics of hydrogenases by ultrafast and two-dimensional infrared spectroscopy

2019 ◽  
Vol 10 (39) ◽  
pp. 8981-8989 ◽  
Author(s):  
Marius Horch ◽  
Janna Schoknecht ◽  
Solomon L. D. Wrathall ◽  
Gregory M. Greetham ◽  
Oliver Lenz ◽  
...  
Keyword(s):  
Infrared Spectroscopy ◽  
Two Dimensional ◽  
Proof Of Concept ◽  
Concept Study ◽  
Structure And Dynamics ◽  
Two Dimensional Infrared Spectroscopy

A proof-of-concept study on a catalytic [NiFe] intermediate reveals structural and dynamical details of hydrogenases by ultrafast and two-dimensional infrared spectroscopies.

Structure and dynamics of two-dimensional oval configurations

1990 ◽  
Vol 170 (1-2) ◽  
pp. 381-383 ◽  
Author(s):  
K. O. Thielheim
Keyword(s):  
Two Dimensional ◽  
Structure And Dynamics

Selective dismantling of closo-1,2-C2B10H12 to lower-cage dicarbaborane systems

1991 ◽  
Vol 56 (8) ◽  
pp. 1618-1635 ◽  
Author(s):  
Jaromír Plešek ◽  
Bohumil Štíbr ◽  
Xavier L. R. Fontaine ◽  
John D. Kennedy ◽  
Stanislav Heřmánek ◽  
...  
Keyword(s):  
Nmr Spectroscopy ◽  
Solution Structure ◽  
High Yield ◽  
Two Dimensional ◽  
Oxidizing Agents ◽  
Elimination Reactions

A modified, high-yield synthesis of the two isomeric nido twelve-vertex [C2B10H13]- anions, "reactive" [nido-7,9-C2B10H13]- and "unreactive" [nido-7,12-C2B10H13]-, has been developed. A solution structure for the reactive [nido-7,9-C2H10B13]- isomer is proposed on the basis of the result of two-dimensional 11B and 1H correlation NMR spectroscopy. It is concluded that there is a marked similarity between this species and the eleven-vertex congener [nido-7,8-C2B9H12]-. In accord with this parallel, the "reactive" twelve-vertex species is found to undergo selective boron-vertex elimination reactions in the presence of oxidizing agents. These reactions give excellent yields of smaller-cage nido dicarbaborane compounds, namely [nido-7,8-C2B9H12]-, [9-(SMe2)-nido-7,8-C2B9H11], and nido-5,6-C2B8H12. NMR spectroscopy assigns cluster 11B and 1H resonances for all the compounds isolated, and thence permits comparison with the equivalent shielding patterns of structurally related analogues such as [nido-7-CB10H13]- and [nido-7,9-C2B9H12]-.

Investigating exciton structure and dynamics in colloidal CdSe quantum dots with two-dimensional electronic spectroscopy

2018 ◽  
Vol 149 (7) ◽  
pp. 074702 ◽  
Author(s):  
H. Seiler ◽  
S. Palato ◽  
P. Kambhampati
Keyword(s):  
Quantum Dots ◽  
Electronic Spectroscopy ◽  
Cdse Quantum Dots ◽  
Two Dimensional ◽  
Structure And Dynamics

Solution structure and dynamics of glia maturation factor from Caenorhabditis elegans

2018 ◽  
Vol 1866 (10) ◽  
pp. 1008-1020 ◽  
Author(s):  
Diva Maheshwari ◽  
Vaibhav Kumar Shukla ◽  
Anupam Jain ◽  
Sarita Tripathi ◽  
Dinesh Kumar ◽  
...  
Keyword(s):  
Caenorhabditis Elegans ◽  
Solution Structure ◽  
Glia Maturation Factor ◽  
Structure And Dynamics ◽  
Maturation Factor

scholarly journals Unraveling the structure and dynamics of the human DNAJB6b chaperone by NMR reveals insights into Hsp40-mediated proteostasis

2019 ◽  
Vol 116 (43) ◽  
pp. 21529-21538 ◽  
Author(s):  
Theodoros K. Karamanos ◽  
Vitali Tugarinov ◽  
G. Marius Clore
Keyword(s):  
Solution Structure ◽  
Specific Substrate ◽  
Monomeric Form ◽  
Linker Region ◽  
Structure And Dynamics ◽  
J Domain ◽  
Folded Proteins ◽  
High Flexibility ◽  
Interdomain Interactions ◽  
Shed Light

J-domain chaperones are involved in the efficient handover of misfolded/partially folded proteins to Hsp70 but also function independently to protect against cell death. Due to their high flexibility, the mechanism by which they regulate the Hsp70 cycle and how specific substrate recognition is performed remains unknown. Here we focus on DNAJB6b, which has been implicated in various human diseases and represents a key player in protection against neurodegeneration and protein aggregation. Using a variant that exists mainly in a monomeric form, we report the solution structure of an Hsp40 containing not only the J and C-terminal substrate binding (CTD) domains but also the functionally important linkers. The structure reveals a highly dynamic protein in which part of the linker region masks the Hsp70 binding site. Transient interdomain interactions via regions crucial for Hsp70 binding create a closed, autoinhibited state and help retain the monomeric form of the protein. Detailed NMR analysis shows that the CTD (but not the J domain) self-associates to form an oligomer comprising ∼35 monomeric units, revealing an intricate balance between intramolecular and intermolecular interactions. The results shed light on the mechanism of autoregulation of the Hsp70 cycle via conserved parts of the linker region and reveal the mechanism of DNAJB6b oligomerization and potentially antiaggregation.

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