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 The Secondary Structure of Calcineurin Regulatory Region and Conformational Change Induced by Calcium/Calmodulin Binding

2008 ◽  
Vol 283 (17) ◽  
pp. 11407-11413 ◽  
Author(s):  
Xianrong Shen ◽  
Huiming Li ◽  
Yan Ou ◽  
Wenbing Tao ◽  
Aichun Dong ◽  
...  
Keyword(s):  
Secondary Structure ◽  
Conformational Change ◽  
Regulatory Region ◽  
Calmodulin Binding

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
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