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Hyperhelical Actuators: Coils and Coiled-Coils
45th AIAA/ASME/ASCE/AHS/ASC Structures, Structural Dynamics & Materials Conference, 2004This study is concerned with multiply coiled, hierarchical structures, known formally as hyperhelices, for use as large displacement, solid-state actuators. They are made by curving thin strips of active material into successively larger helicoidal forms. The degree of shape change for any hyperhelix is obtained from the recursive solution of a pair of
K Seffen, E Toews
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A Coiled Coil with a Fluorous Core
Journal of the American Chemical Society, 2001The design, synthesis, and structural characterization of a highly fluorinated peptide system based on the coiled coil region of the yeast transcription factor GCN4 is described. All four leucine residues (a position) and three valine residues (d position) were replaced by the unnatural amino acids 5,5,5-trifluoroleucine and 4,4,4-trifluorovaline ...
B, Bilgiçer, A, Fichera, K, Kumar
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A Designed Heterotrimeric Coiled Coil
Biochemistry, 1995Principles that guide folding of coiled coils were tested by designing three peptides that preferentially associate with each other to form a heterotrimeric coiled coil. The core positions of the designed helices contained residues that promote formation of trimeric coiled coils.
S, Nautiyal +3 more
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Coiled coils meet the chaperone world
Trends in Biochemical Sciences, 2004Coiled coils are versatile structural modules that engage in a variety of cellular activities. Recent studies illuminate their role as substrate-binding elements in the chaperone cofactor prefoldin and in the AAA+ ATPases involved in protein (un)folding processes.
Jörg, Martin +2 more
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Engineered Coiled-Coil Protein Microfibers
Biomacromolecules, 2014The fabrication of de novo proteins able to self-assemble on the nano- to meso-length scales is critical in the development of protein-based biomaterials in nanotechnology and medicine. Here we report the design and characterization of a protein engineered coiled-coil that not only assembles into microfibers, but also can bind hydrophobic small ...
Jasmin, Hume +7 more
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Evidence That the Leucine Zipper Is a Coiled Coil
Science, 1989Recently, a hypothetical structure called a leucine zipper was proposed that defines a new class of DNA binding proteins. The common feature of these proteins is a region spanning approximately 30 amino acids that contains a periodic repeat of leucines every seven residues.
E K, O'Shea, R, Rutkowski, P S, Kim
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Predicting coiled-coil regions in proteins
Current Opinion in Structural Biology, 1997The past several years have seen significant advances in our ability to recognize coiled coils from protein sequences and model their structures. New methods include a detection program based on pairwise residue correlations, a program that distinguishes two-stranded from three-stranded coiled coils and a routine for modelling the coordinates of the ...
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Coiled-Coil Design: Updated and Upgraded
2017α-Helical coiled coils are ubiquitous protein-folding and protein-interaction domains in which two or more α-helical chains come together to form bundles. Through a combination of bioinformatics analysis of many thousands of natural coiled-coil sequences and structures, plus empirical protein engineering and design studies, there is now a deep ...
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Coiled-coils and fibrous proteins
Journal of Structural Biology, 2010David A D, Parry, John M, Squire
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