Observance of a large conformational change associated with the rotation of the naphthyl groups during the photodimerization of criss-cross aligned CC bonds within a 2D coordination polymer

CrystEngComm ◽  
2015 ◽  
Vol 17 (26) ◽  
pp. 4903-4911 ◽  
Author(s):  
Fei-Long Hu ◽  
Shu-Long Wang ◽  
Brendan F. Abrahams ◽  
Jian-Ping Lang
Keyword(s):  
Coordination Polymer ◽  
Conformational Change ◽  
Large Conformational Change

scholarly journals Light and heat control over secondary structure and amyloid-like fiber formation in an overcrowded-alkene-modified Trp zipper

2015 ◽  
Vol 6 (12) ◽  
pp. 7311-7318 ◽  
Author(s):  
Claudia Poloni ◽  
Marc C. A. Stuart ◽  
Pieter van der Meulen ◽  
Wiktor Szymanski ◽  
Ben L. Feringa
Keyword(s):  
Secondary Structure ◽  
Conformational Change ◽  
Fiber Formation ◽  
Major Influence ◽  
Heat Control ◽  
Large Conformational Change

The use of an overcrowded alkene photoswitch to control a model β-hairpin peptide is described. The light-induced, large conformational change has major influence on the secondary structure and the aggregation of the peptide, permitting the triggered formation of amyloid-like fibrils.

scholarly journals A microtubule-dynein tethering complex regulates the axonemal inner dynein f (I1)

2018 ◽  
Vol 29 (9) ◽  
pp. 1060-1074 ◽  
Author(s):  
Tomohiro Kubo ◽  
Yuqing Hou ◽  
Deborah A. Cochran ◽  
George B. Witman ◽  
Toshiyuki Oda
Keyword(s):  
Conformational Change ◽  
Molecular Mechanism ◽  
Wild Type ◽  
Sliding Direction ◽  
Large Conformational Change ◽  
Dynein Arms ◽  
Biochemical Analyses

Motility of cilia/flagella is generated by a coordinated activity of thousands of dyneins. Inner dynein arms (IDAs) are particularly important for the formation of ciliary/flagellar waveforms, but the molecular mechanism of IDA regulation is poorly understood. Here we show using cryoelectron tomography and biochemical analyses of Chlamydomonas flagella that a conserved protein FAP44 forms a complex that tethers IDA f (I1 dynein) head domains to the A-tubule of the axonemal outer doublet microtubule. In wild-type flagella, IDA f showed little nucleotide-dependent movement except for a tilt in the f β head perpendicular to the microtubule-sliding direction. In the absence of the tether complex, however, addition of ATP and vanadate caused a large conformational change in the IDA f head domains, suggesting that the movement of IDA f is mechanically restricted by the tether complex. Motility defects in flagella missing the tether demonstrates the importance of the IDA f-tether interaction in the regulation of ciliary/flagellar beating.

scholarly journals Structure of human thioredoxin exhibits a large conformational change

2010 ◽  
Vol 19 (9) ◽  
pp. 1807-1811 ◽  
Author(s):  
Gareth Hall ◽  
Jonas Emsley
Keyword(s):  
Conformational Change ◽  
Large Conformational Change

scholarly journals A large conformational change in the putative ATP pyrophosphatase PF0828 induced by ATP binding

2011 ◽  
Vol 67 (11) ◽  
pp. 1323-1327 ◽  
Author(s):  
Farhad Forouhar ◽  
Nabila Saadat ◽  
Munif Hussain ◽  
Jayaraman Seetharaman ◽  
Insun Lee ◽  
...  
Keyword(s):  
Conformational Change ◽  
Atp Binding ◽  
Large Conformational Change

scholarly journals Conformational analysis of peramivir reveals critical differences between free and enzyme-bound states

MedChemComm ◽  
2014 ◽  
Vol 5 (10) ◽  
pp. 1483-1488 ◽  
Author(s):  
Michele R. Richards ◽  
Michael G. Brant ◽  
Martin J. Boulanger ◽  
Christopher W. Cairo ◽  
Jeremy E. Wulff
Keyword(s):  
Solid State ◽  
Conformational Analysis ◽  
Conformational Change ◽  
Bound States ◽  
Enzyme Binding ◽  
Large Conformational Change ◽  
Conformational Distribution

An analysis of the conformational distribution of peramivir, a potent anti-influenza compound, in solution and the solid state reveals a large conformational change required for enzyme binding.

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