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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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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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Predicting Coiled Coils from Protein Sequences
Science, 1991The probability that a residue in a protein is part of a coiled-coil structure was assessed by comparison of its flanking sequences with sequences of known coiled-coil proteins. This method was used to delineate coiled-coil domains in otherwise globular proteins, such as the leucine zipper domains in transcriptional regulators, and to predict regions ...
Lupas, A. ; https://orcid.org/0000-0002-1959-4836 +2 more
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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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The design of antiparallel coiled coils
Current Opinion in Structural Biology, 2001Recent 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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Coiled‐coil length: Size does matter
Proteins: Structure, Function, and Bioinformatics, 2015ABSTRACTProtein evolution is governed by processes that alter primary sequence but also the length of proteins. Protein length may change in different ways, but insertions, deletions and duplications are the most common. An optimal protein size is a trade‐off between sequence extension, which may change protein stability or lead to acquisition of a new
Jaroslaw Surkont +3 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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Simultaneous acquisition of spatial harmonics (SMASH): Fast imaging with radiofrequency coil arrays
Magnetic Resonance in Medicine, 1997D. Sodickson, W. Manning
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A METHOD OF MEASURING EYE MOVEMENT USING A SCLERAL SEARCH COIL IN A MAGNETIC FIELD.
IEEE transactions on bio-medical engineering, 1963D. A. Robinson
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Comparative Analysis of Two-Coil and Three-Coil Structures for Wireless Power Transfer
IEEE transactions on power electronics, 2017Jian Zhang +3 more
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