scholarly journals How Insect Flight Steering Muscles Work

PLoS Biology ◽  
2014 ◽  
Vol 12 (3) ◽  
pp. e1001822 ◽  
Author(s):  
Anders Hedenström
Keyword(s):  
Insect Flight ◽  
Flight Steering

The Biomechanics of Insect Flight

2018 ◽  
Author(s):  
Robert Dudley
Keyword(s):  
Insect Flight

Critical P2 and insect flight: The role of tracheal volume in the Oogenesis-Flight Syndrome

2021 ◽  
Vol 254 ◽  
pp. 110873
Author(s):  
Tomer Urca ◽  
Eran Gefen ◽  
Gal Ribak
Keyword(s):  
Insect Flight

scholarly journals On the shape of cicada’s wing leading-edge cross section

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Rachel M. Starkweather ◽  
Svetlana V. Poroseva ◽  
David T. Hanson
Keyword(s):  
Cross Section ◽  
Insect Flight ◽  
Leading Edge ◽  
Flight Performance ◽  
Cross Section Shape ◽  
Section Shape ◽  
First Time

AbstractAn important role that the leading-edge cross-section shape plays in the wing flight performance is well known in aeronautics. However, little is known about the shape of the leading-edge cross section of an insect’s wing and its contribution to remarkable qualities of insect flight. In this paper, we reveal, in the first time, the shape of the leading-edge cross section of a cicada’s wing and analyze its variability along the wing. We also identify and quantify similarities in characteristic dimensions of this shape in the wings of three different cicada species.

scholarly journals FLAPPING WING DEVICES FOR MARS EXPLORATION

2011 ◽  
Author(s):  
Asier Ania ◽  
Dominique Poirel ◽  
Marie-Josée Potvin ◽  
Steeve Montminy
Keyword(s):  
Reynolds Number ◽  
Insect Flight ◽  
Low Reynolds Number ◽  
Flapping Wing ◽  
Low Density ◽  
Mars Exploration ◽  
Unsteady Aerodynamic ◽  
Aerial Vehicle ◽  
Low Reynolds

The use of an aerial vehicle would greatly enhance the domain of exploration on Mars. The main constraint in such a design would be the extreme Martian environment. The low-density atmosphere suggests the use of a low Reynolds number flight regime modeled after flapping wing insect flight. This flapping wing flight employs several unsteady aerodynamic mechanisms; delayed stall, wake capture, and rotational mechanisms. Two prototypes, a flapping wing and a rotary-flapping wing hybrid, have been built and will be tested in order to quantify the 'overall lift' generated and allow us to evaluate the efficacy of flapping wing flight on Mars.

Biogenesis of giant mitochondria during insect flight muscle development in the locust, Locusta migratoria (L.)

2000 ◽  
Vol 267 (1) ◽  
pp. 11-17 ◽  
Author(s):  
Bettina Sogl ◽  
Gerd Gellissen ◽  
Rudolf J. Wiesner
Keyword(s):  
Muscle Development ◽  
Flight Muscle ◽  
Insect Flight ◽  
Locusta Migratoria ◽  
Insect Flight Muscle ◽  
Giant Mitochondria

The site of paramyosin in insect flight muscle and the presence of an unidentified protein between myosin filaments and Z-line

1977 ◽  
Vol 115 (3) ◽  
pp. 417-440 ◽  
Author(s):  
Belinda Bullard ◽  
Kathleen S. Hammond ◽  
Barbara M. Luke
Keyword(s):  
Flight Muscle ◽  
Insect Flight ◽  
Insect Flight Muscle ◽  
Myosin Filaments

Cytoskeletal proteins of insect muscle: location of zeelins in Lethocerus flight and leg muscle

1994 ◽  
Vol 107 (5) ◽  
pp. 1115-1129 ◽  
Author(s):  
C. Ferguson ◽  
A. Lakey ◽  
A. Hutchings ◽  
G.W. Butcher ◽  
K.R. Leonard ◽  
...  
Keyword(s):  
Insect Flight ◽  
Regular Structure ◽  
Thick Filament ◽  
Cytoskeletal Proteins ◽  
Stretch Activation ◽  
Insect Muscle ◽  
Thick Filaments ◽  
Flight Muscles ◽  
Leg Muscle ◽  
Low Ionic Strength

Asynchronous insect flight muscles produce oscillatory contractions and can contract at high frequency because they are activated by stretch as well as by Ca2+. Stretch activation depends on the high stiffness of the fibres and the regular structure of the filament lattice. Cytoskeletal proteins may be important in stabilising the lattice. Two proteins, zeelin 1 (35 kDa) and zeelin 2 (23 kDa), have been isolated from the cytoskeletal fraction of Lethocerus flight muscle. Both zeelins have multiple isoforms of the same molecular mass and different charge. Zeelin 1 forms micelles and zeelin 2 forms filaments when renatured in low ionic strength solutions. Filaments of zeelin 2 are ribbons 10 nm wide and 3 nm thick. The position of zeelins in fibres from Lethocerus flight and leg muscle was determined by immunofluorescence and immunoelectron microscopy. Zeelin 1 is found in flight and leg fibres and zeelin 2 only in flight fibres. In flight myofibrils, both zeelins are in discrete regions of the A-band in each half sarcomere. Zeelin 1 is across the whole A-band in leg myofibrils. Zeelins are not in the Z-disc, as was thought previously, but migrate to the Z-disc in glycerinated fibres. Zeelins are associated with thick filaments and analysis of oblique sections showed that zeelin 1 is closer to the filament shaft than zeelin 2. The antibody labelling pattern is consistent with zeelin molecules associated with myosin near the end of the rod region. Alternatively, the position of zeelins may be determined by other A-band proteins. There are about 2.0 to 2.5 moles of myosin per mole of each zeelin. The function of these cytoskeletal proteins may be to maintain the ordered structure of the thick filament.

A method for determining the periodicity of a troponin component in isolated insect flight muscle thin filaments by gold/Fab labelling

1992 ◽  
Vol 101 (3) ◽  
pp. 503-508
Author(s):  
R. Newman ◽  
G.W. Butcher ◽  
B. Bullard ◽  
K.R. Leonard
Keyword(s):  
Gold Particle ◽  
Colloidal Gold ◽  
Striated Muscle ◽  
Flight Muscle ◽  
Insect Flight ◽  
Insect Flight Muscle ◽  
Fab Fragment ◽  
Thin Filaments ◽  
Gold Particles ◽  
Almost All

Insect flight muscle has a large component (Tn-H) in the tropomyosin-troponin complex that is not present in vertebrate striated muscle thin filaments. Tn-H is shown by gold/Fab labelling to be present at regular intervals in insect flight muscle thin filaments. The Fab fragment of a monoclonal antibody to Tn-H was conjugated directly with colloidal gold and this probe used to label isolated thin filaments from the flight muscle of Lethocerus indicus (water bug). The distribution of gold particles seen in electron microscope images of negatively stained thin filaments was analysed to show that the probe bound to sites having a periodicity of approximately 40 nm, which is the expected value for the tropomyosin-troponin repeat. Conjugates of Fab with colloidal gold particles of 3 nm diameter labelled almost all sites. Conjugates with gold particles of 5 nm and 10 nm diameter labelled less efficiently (70% and 30%, respectively) but analysis of the distribution of inter-particle intervals among a number of filaments again gave the same fundamental spacing of 40 nm. The error in the measurements (standard deviation approximately +/− 4.2 for 5 nm gold/Fab) is less than earlier estimates for the size of the gold/Fab complex. Measurements on gold/Fab in negative stain suggest that the bound Fab contributes a shell about 2 nm in thickness around the gold particle. The radius of the probe (about 4.5 nm for 5 nm gold/Fab) would then be consistent with the value of error found. The size of the probe suggests that the gold particle binds to the side of the Fab molecule, rather close to the antibody combining site. The potential resolution of the technique may thus be better than originally expected.

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