The coiled coil-helix-coiled coil-helix proteins may be redox proteins
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چکیده
منابع مشابه
A seven-helix coiled coil.
Coiled-coil proteins contain a characteristic seven-residue sequence repeat whose positions are designated a to g. The interacting surface between alpha-helices in a classical coiled coil is formed by interspersing nonpolar side chains at the a and d positions with hydrophilic residues at the flanking e and g positions. To explore how the chemical nature of these core amino acids dictates the o...
متن کاملThe coiled-coil helix in the neck of kinesin.
Kinesin is a microtubule-dependent motor protein. We have recently determined the X-ray structure of monomeric and dimeric kinesin from rat brain. The dimer consists of two motor domains, held together by their alpha-helical neck domains forming a coiled coil. Here we analyze the nature of the interactions in the neck domain (residues 339-370). Overall, the neck helix shows a heptad repeat (abc...
متن کاملFTIR-Spectroscopy of multistranded coiled coil proteins.
Coiled coils of different order were investigated using infrared (IR) spectroscopy. Recently, we demonstrated that dimeric coiled coils display unique vibrational spectra with at least three separable bands instead of only one band of a classical alpha-helix in the amide I region. This was attributed to a distortion of the helical structure by the supercoil bending, giving rise to bands that ar...
متن کاملPredicting coiled-coil regions in proteins.
The 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 core residues in coiled coils. Several widely...
متن کاملHelix-Coil Transitions of a-Helical, Two-Chain, Coiled Coils
A theory of the helix-coil transition for in-register, two-chain, a-helical, coiled coils such as tropomyosin and paramyosin is developed. The treatment differs from those formulated previously for DNAor collagen-like double helices; in the present treatment, isolated single chains and each of the two strands in the dimer may be partially helical. We calculate the fraction of helix in the two-c...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 2009
ISSN: 0014-5793
DOI: 10.1016/j.febslet.2009.03.061