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F A Blyakhman

Publications and source records attributed to F A Blyakhman.

3 recordsLinked to original sources

'Minimum average risk' as a new peak-detection algorithm applied to myofibrillar dynamics.

We present a new peak-detection algorithm based on the method of 'minimum average risk' proposed by Kolmogorov and developed for signal processing in various fields. In this method, translations of features within a signal scan are quantified by minimizing the integrated pointwise product of each scan relative to the first derivative of the immediately previous scan. We have adapted this method for use in a new algorithm to monitor dynamic changes of sarcomere length in single myofibrillar sarcomeres of striated muscles, but the algorithm can also be used more generally for peak localization. We find that this method results in sub-nanometer precision and higher signal-to-noise ratio than current methods. At an equal noise level, the RMS deviation of the minimum average risk algorithm was 1.3 times lower than that of the center of mass method with modeled data and 3-4 times lower with actual data.

Algorithms↗

Quantal length changes in single contracting sarcomeres.

The time course of shortening was investigated in the single sarcomere, the smallest contractile unit that retains natural structure. We projected the striation patterns of single bumblebee flight-muscle myofibrils onto a linear photodiode array, which was scanned periodically to produce repetitive traces of intensity vs. position along the array. Sarcomere length was taken as the span between adjacent A-band or Z-line centroids. When myofibrils were ramp-released by a motor, individual sarcomeres shortened in steps punctuated by pauses. The single sarcomere-shortening trace was consistently stepwise both in activated and relaxed specimens. Although step size was variable, the size distribution showed a signature-like feature: the histogram comprised distinct peaks that were spaced quasi-regularly. In the activated myofibrils the interpeak separation corresponded to 2.71 nm per half-sarcomere. This value is equal to the linear advance of actin subunits along the thin filament. Thus, actin filaments translate over thick filaments by steps that may be integer multiples of the actin-subunit spacing.

Actins↗

Cooperative effects due to calcium binding by troponin and their consequences for contraction and relaxation of cardiac muscle under various conditions of mechanical loading.

A mathematical model for the regulation of mechanical activity in cardiac muscle has been developed based on a three-element rheological model of this muscle. The contractile element has been modeled taking into account the results of extensive mechanical tests that involved the recording of length-force and force-velocity relations and muscle responses to short-time deformations during various phases of the contraction-relaxation cycle. The best agreement between the experimental and the mathematical modeling results was obtained when a postulate stating two types of cooperativity to regulate the calcium binding by troponin was introduced into the model. Cooperativity of the first type is due to the dependence of the affinity of troponin C for Ca2+ on the concentration of myosin crossbridges in the vicinity of a given troponin C. Cooperativity of the second type assumes an increase in the affinity of a given troponin C for Ca2+ when the latter is bound by molecules neighboring troponin.

Animals↗