protofilament

pro·to·fil·a·ment

(prō'tō-fil'ă-ment),
Basic element of a contractile flagellar microtubule, approximately 5 nm thick.
[proto- + L. filum, a thread]
Farlex Partner Medical Dictionary © Farlex 2012
Mentioned in ?
References in periodicals archive ?
Hayashi et al., "Toll-like receptor 5 recognizes a conserved site on flagellin required for protofilament formation and bacterial motility," Nature Immunology, vol.
These differences can be seen in (i) the length of the [beta]-strands, (ii) the arrangement (parallel versus antiparallel) of the constituting sheets of the strand, (iii) the length and arrangement of structures which are not inside the fibril core, and (iv) the number of [beta]-sheets per each protofilament [1].
The lateral contacts involve the interactions of 1-11S2 loop and helix H3 with the M-loop of the adjacent protofilament. Thus, 13 protofilaments associate laterally and are found to be more electrostatic and less hydrophobic than the longitudinal contacts (2-6).
Considering that a microtubule consists of 13 protofilaments and each [alpha][beta] tubulin dimer adds approximately 8 nm to the length of a protofilament, the growth of 24 nm and 48 nm of a microtubule consumes 39 ((24/8) x 13) and 78 ((48/8) x 13) tubulin dimers, respectively.
The protofilament building blocks of Al tangles also differ from those of AD with the diameter of the former 2.0 nm and the latter 3.2 nm.
The released energy is then stored in the microtubule wall as an elastic strain, and the [beta]--tubulin bound GDP cannot be further phosphorylated or exchanged for GTP because the successive [alpha]--tubulin in the protofilament occludes the preceding [beta]--tubulin nucleotide binding pocket (Heald and Nogales, 2002).
The growth phase is governed by the presence of a tubulin GTP cap at the end of the microtubule, and the structure we observe is tubulin protofilament sheet folded up into a blunt and straight microtubule.
The actin filament has a two-stranded helical structure, called a protofilament, which contains 7 monomers and rotates 180[degrees] per half helical pitch.
Each single monomer then interacts with another, as a pair, via the side chains of residues 26 to 32, thus forming the single protofilament. Protofilaments then laterally associate, leading to the mature fibril [6].
The protofilament building block of the amylin fibril structure [13] has two [C.sub.2]-symmetry related stacks of intermolecular [beta]-sheets (shown in orange and purple in Figure 1(b)).