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Kinking the Coiled Coil – Negatively Charged Residues at the Coiled-coil Interface
Journal of Molecular Biology, 2007The coiled coil is one of the most common protein-structure motifs. It is believed to be adopted by 3-5% of all amino acids in proteins. It comprises two or more alpha-helical chains wrapped around one another. The sequences of most coiled coils are characterized by a seven-residue (heptad) repeat, denoted (abcdefg)(n).
Straussman, R +3 more
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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 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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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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The Structure of α-Helical Coiled Coils
2005alpha-Helical coiled coils are versatile protein domains, supporting a wide range of biological functions. Their fold is probably better understood than that of any other protein; indeed, uniquely among folds, their structure can be computed from a set of parametric equations. Here, we review the principles of coiled-coil structure, the determinants of
Lupas, A. ; https://orcid.org/0000-0002-1959-4836 +1 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.
Martin, J. ; https://orcid.org/0000-0003-1398-0274 +2 more
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Short Homodimeric and Heterodimeric Coiled Coils
Biomacromolecules, 2006In this communication, we discuss the design, synthesis, and characterization of four peptides which are able to self-assemble into five different homo- and heterodimeric alpha-helical coiled coils based on the pH of their environment. These peptides are very short, containing only 14 or 21 amino acids each, and illustrate the minimum requirements ...
He, Dong, Jeffrey D, Hartgerink
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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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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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