scholarly journals The Structure of the Cyclodextrin Complex. XIX. Crystal Structures of Hexakis(2,3,6-tri-O-methyl)-α-cyclodextrin Complexes with (S)- and (R)-Mandelic Acid. Chiral Recognition through the Induced-Fit Conformational Change of the Macrocyclic Ring

1987 ◽  
Vol 60 (2) ◽  
pp. 497-502 ◽  
Author(s):  
Kazuaki Harata ◽  
Kaneto Uekama ◽  
Masaki Otagiri ◽  
Fumitoshi Hirayama
Keyword(s):  
Crystal Structures ◽  
Conformational Change ◽  
Mandelic Acid ◽  
Chiral Recognition ◽  
Cyclodextrin Complexes ◽  
Cyclodextrin Complex ◽  
Induced Fit ◽  
Macrocyclic Ring

Highly nonplanar macrocyclic ring conformation in the crystal structures of Ni(II) and Cu(II) octaphenylporphyrins

2018 ◽  
Vol 59 (2) ◽  
Author(s):  
P. Bhyrappa ◽  
◽  
M. Sankar ◽  
K. Karunanithi ◽  
B. Varghese ◽  
...  
Keyword(s):  
Crystal Structures ◽  
Ring Conformation ◽  
Macrocyclic Ring

Chiral Recognition of Racemic Proline based on Chiral Macrocyclic Nickel(II) Complex: Synthesis and Crystal Structures

2018 ◽  
Vol 644 (8-9) ◽  
pp. 449-453 ◽  
Author(s):  
Huan-Yong Li ◽  
Guo-Kai Jia ◽  
Fei Zeng ◽  
Shan-Shan Tang ◽  
Guang-Chuan Ou
Keyword(s):  
Crystal Structures ◽  
Chiral Recognition ◽  
Macrocyclic Nickel

scholarly journals Crystal structures of PI3K-C2α PX domain indicate conformational change associated with ligand binding

2008 ◽  
Vol 8 (1) ◽  
pp. 13 ◽  
Author(s):  
Gary N Parkinson ◽  
David Vines ◽  
Paul C Driscoll ◽  
Snezana Djordjevic
Keyword(s):  
Ligand Binding ◽  
Crystal Structures ◽  
Conformational Change ◽  
Px Domain

The complexation of glucose and other monosaccharides with cyclodextrins

1997 ◽  
Vol 75 (1) ◽  
pp. 52-55 ◽  
Author(s):  
Frank Hacket ◽  
Jose-Miguel Coteron ◽  
Hans-Jörg Schneider ◽  
Vladimir P. Kazachenko
Keyword(s):  
Molecular Modelling ◽  
Equilibrium Constants ◽  
Association Constants ◽  
Cyclodextrin Complexes ◽  
Cyclodextrin Complex ◽  
Intermolecular Hydrogen Bonds ◽  
Calorimetric Measurements ◽  
Computer Aided ◽  
Molecular Modelling Studies ◽  
Modelling Studies

Equilibrium constants of complexes between β-cyclodextrin and glucose, galactose, or mannose have been determined by fluorometric competition titrations in water to be as low as K = 1 – 0.5 M−1, in sharp contrast to recently published values for glucose around K = 400 M–1. The pentoses ribose, xylose, and arabinose show association constants between 6.3 and 1.5 M−1, in agreement with published values. Preliminary computer-aided molecular modelling studies suggest that the small values observed for the hexoses are not due to steric hindrance of an intracavity inclusion but to a smaller number of intermolecular hydrogen bonds and to some strain as a result of cyclodextrin deformation. Calorimetric measurements of the glucose–β-cyclodextrin complex show, again in contradiction with the literature, an endothermic reaction, or a free enthalpy value close to zero. Key words: cyclodextrin complexes, sugar complexation, glucose complexation, calorimetry, computer-aided molecular modelling.

scholarly journals Fabrication of bio-based polyurethane nanofibers incorporated with a triclosan/cyclodextrin complex for antibacterial applications

RSC Advances ◽  
2020 ◽  
Vol 10 (6) ◽  
pp. 3450-3458 ◽  
Author(s):  
Joo Hyung Lee ◽  
Sang Ho Park ◽  
Seong Hun Kim
Keyword(s):  
Antibacterial Properties ◽  
Cyclodextrin Complexes ◽  
Cyclodextrin Complex ◽  
Electrospinning Method

Bio-polyurethane nanofibers containing triclosan–cyclodextrin complexes to enhance antibacterial properties were prepared using an electrospinning method.

scholarly journals Ligand-induced Conformational Shift in the N-terminal Domain of GRP94, an Hsp90 Chaperone

2004 ◽  
Vol 279 (44) ◽  
pp. 46162-46171 ◽  
Author(s):  
Robert M. Immormino ◽  
D. Eric Dollins ◽  
Paul L. Shaffer ◽  
Karen L. Soldano ◽  
Melissa A. Walker ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Crystal Structures ◽  
Conformational Change ◽  
Atp Hydrolysis ◽  
Dna Gyrase ◽  
Regulatory Domain ◽  
Conformational Switch ◽  
Terminal Ligand ◽  
Conformational Rearrangement ◽  
Hsp90 Chaperone

GRP94 is the endoplasmic reticulum paralog of cytoplasmic Hsp90. Models of Hsp90 action posit an ATP-dependent conformational switch in the N-terminal ligand regulatory domain of the chaperone. However, crystal structures of the isolated N-domain of Hsp90 in complex with a variety of ligands have yet to demonstrate such a conformational change. We have determined the structure of the N-domain of GRP94 in complex with ATP, ADP, and AMP. Compared with theN-ethylcarboxamidoadenosine and radicicol-bound forms, these structures reveal a large conformational rearrangement in the protein. The nucleotide-bound form exposes new surfaces that interact to form a biochemically plausible dimer that is reminiscent of those seen in structures of MutL and DNA gyrase. Weak ATP binding and a conformational change in response to ligand identity are distinctive mechanistic features of GRP94 and suggest a model for how GRP94 functions in the absence of co-chaperones and ATP hydrolysis.

Sign in / Sign up

Export Citation Format

Share Document