Titin: quantitative mass measurements by scanning transmission electron microscopy and structural implications for the sarcomere matrix of skeletal muscle.
Scanning transmission electron microscopy has been used to investigate mass and linear mass density of native titin-2, a large soluble fragment of intact titin, from rabbit skeletal muscle. Dark field images of unstained, freeze-dried titin-2 appeared as either compact globules or looser and larger balls of string. Direct mass measurements indicated that the compact forms have an average mass of 2.40 +/- 0.50 x 10(6) Da. The mass to length ratio, determined from well-spread portions of titin strands (3-5 nm wide) from the ball of string forms, averaged 2.7 +/- 0.9 kDa/nm. Thus a single native intact titin molecule has a calculated contour length of well above approximately 1 micron, sufficient to span unidirectionally between the Z line and M line region in a resting-length sarcomere.
Hainfeld
J F
JF
Department of Biology, Brookhaven National Laboratory, Upton, NY 11973.
Wall
J S
JS
Wang
K
K
D000818:Animals; D002352:Carrier Proteins; D064211:Connectin; D008565:Membrane Proteins / Q000032:analysis; D008855:Microscopy, Electron, Scanning; D009124:Muscle Proteins / Q000032:analysis*; D009132:Muscles / Q000032:analysis* / Q000648:ultrastructure; D009210:Myofibrils / Q000648:ultrastructure*; D011494:Protein Kinases; D011817:Rabbits; D012518:Sarcomeres / Q000648:ultrastructure*
D002352:Carrier Proteins; D064211:Connectin; D008565:Membrane Proteins; D009124:Muscle Proteins; D011494:Protein Kinases