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Articles by William J. Lehman
Protein-protein docking reveals dynamic interactions of tropomyosin on actin filaments
Abstract Experimental approaches, such as fiber diffraction and cryo-electron microscopy reconstruction, have defined regulatory positions of tropomyosin on actin, but have not as yet succeeded at determining key atomic-level contacts between these proteins or fully substantiated the dynamics of their interactions at a structural level.
Introducing a special issue of the Journal of Muscle Research and Cell Motility on actin and actin-binding proteins
The 47th annual European Muscle Conference was held at the Basic Medical Science Center of Semmelweis University in beautiful and historic Budapest. One session of the conference was devoted to “Actin and Actin-Binding Proteins”. What better place to hold this session than in “Albert Szent-Györgyi Hall” at Semmelweis. After all it was in the Szent-Györgyi laboratory in Szeged (Fig.
CARDIOMYOPATHY MUTATION ALTERS END-TO-END JUNCTION OF TROPOMYOSIN AND REDUCES CALCIUM SENSITIVITY
Abstract Muscle contraction is governed by tropomyosin (Tpm) shifting azimuthally between three states on F-actin (Blocked, Closed and Open) in response to calcium-binding to troponin and acto-myosin cross-bridge formation. The Tpm coiled coil polymerizes head-to-tail along the long-pitch helix of F-actin to form continuous super-helical cables that wrap around the actin filaments.
The Effect of Tropomyosin Mutations on Actin-Tropomyosin Binding: In Search of Lost Time
Abstract The initial binding of tropomyosin onto actin filaments and then its polymerization into continuous cables on the filament surface must be precisely tuned to overall thin filament structure, function and performance. Low-affinity interaction of tropomyosin with actin has to be sufficiently strong to localize the tropomyosin on actin, yet not so tight that regulatory movement on filaments is curtailed.
A new twist on tropomyosin binding to actin filaments: perspectives on thin filament function, assembly and biomechanics
Article First Online: 15 February 2019 Abstract Tropomyosin, best known for its role in the steric regulation of muscle contraction, polymerizes head-to-tail to form cables localized along the length of both muscle and non-muscle actin-based thin filaments.
Precise Binding of Tropomyosin on Actin Involves Sequence-Dependent Variance in Coiled-coil Twisting
Often considered an archetypal dimeric coiled-coil, tropomyosin nonetheless exhibits distinctive “non-canonical” core residues located at the hydrophobic interface between its component α-helices. Notably, a charged aspartate, D137, takes the place of non-polar residues otherwise present. Much speculation has been offered to rationalize potential local coiled-coil instability stemming from D137 and its effect on regulatory transitions of tropomyosin over actin filaments.
Switching Muscles On and Off in Steps: The McKillop-Geeves Three-State Model of Muscle Regulation
Publication HistoryEditor: E. Ostap.Accepted: April 21, 2017; Received: April 6, 2017;
William J. Lehman - Daily Star-Journal: Obituaries
William was born Sept. 22, 1944, in Washington, Indiana, son of Clifford T. and Thelma E. (Keasling) Lehman. He was raised in Bruceville, Indiana, where he graduated from high school. He enlisted in the United States Air Force in 1962, and he was stationed at Takli A.F.B., Thailand. William was united in marriage to Joyce A. Crouse on July 2, 1966, in Bruceville. Shortly after, he was stationed at Scott A.F.B., Illinois. The next year, he was reassigned to Bien Hoa A.F.B., Vietnam.
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