Results 261 to 270 of about 29,669 (308)

A resolution for the coiling direction paradox inNeogloboquadrina pachyderma [PDF]

Paleoceanography, 2006
We present new data on genotypic differences and biogeographic distribution of coiling types in the living planktonic foraminiferal morphospecies Neogloboquadrina pachyderma. The genetic evidence demonstrates that coiling direction in N.
Kate F Darling, Michal Kučera, Dick Kroon   +2 more
exaly   +2 more sources

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Coils

Computer Aided Geometric Design, 1996
zbMATH Open Web Interface contents unavailable due to conflicting licenses.
Caroline Labenski, Bruce R. Piper
openaire   +1 more source

Kinking the Coiled Coil – Negatively Charged Residues at the Coiled-coil Interface

Journal of Molecular Biology, 2007
The 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, Ben-Ya'acov, A, Woolfson, DN, Ravid, S   +3 more
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Hyperhelical Actuators: Coils and Coiled-Coils

45th AIAA/ASME/ASCE/AHS/ASC Structures, Structural Dynamics & Materials Conference, 2004
This 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
openaire   +1 more source

A Coiled Coil with a Fluorous Core

Journal of the American Chemical Society, 2001
The 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
openaire   +2 more sources

The design of antiparallel coiled coils

Current Opinion in Structural Biology, 2001
Recent structural studies have highlighted the importance of antiparallel coiled coils in nature. In addition, well-behaved, model antiparallel coiled coils have been designed and used for the reassembly of protein fragments and for the study of the energetic contributions of various interactions to helix orientation specificity.
M G, Oakley, J J, Hollenbeck
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A Designed Heterotrimeric Coiled Coil

Biochemistry, 1995
Principles 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, D N, Woolfson, D S, King, T, Alber   +3 more
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Coiled coils meet the chaperone world

Trends in Biochemical Sciences, 2004
Coiled 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, Markus, Gruber, Andrei N, Lupas   +2 more
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