Tryptic and chymotryptic light meromyosin paracrystals from red and cardiac muscles of rabbit show a negative and positive staining pattern with uranyl acetate and phosphotungstate that sharply differs from that of white muscle light meromyosin paracrystals. The main periodicity of about 430 A is the same regardless of the source of light meromyosin. The results are discussed in terms of the molecular structure and the functional properties of various myosins.. ...

TY - JOUR. T1 - Isolating and localizing ATP-sensitive tryptophan emission in skeletal myosin subfragment 1. AU - Park, S.. AU - Burghardt, T. P.. N1 - Copyright: Copyright 2011 Elsevier B.V., All rights reserved.. PY - 2000/9/26. Y1 - 2000/9/26. N2 - The fluorescence intensity difference between rabbit skeletal myosin subfragment 1 (S1) and nucleotide-bound or trapped S1 isolates ATP-sensitive tryptophans (ASTs) emission from the total tryptophan signal. Neutral (acrylamide) quenching of the ASTs is sensitive to the binding or trapping of nucleotide to the active site of S1. Anion (I-) quenching of the ASTs, sensitive to charge separation in the tryptophan micro environment, is negligible. These findings suggest the ASTs sense conformational change during ATPase from negatively charged surroundings. Specific chemical modifications of S1 identified the location of the ASTs. Trp131 was quenched by chemical modification, and its emission was isolated by taking the intensity difference between ...

Enzymatic studies on the interaction of myosin and heavy meromyosin with 1,N 6- ethenoadenosine triphosphate (ATP), a fluorescent analogue of ATP: Biochem.Biophys.Res.Commun.

We have used actin labelled at Cys-374 with N-(1-pyrenyl)iodoacetamide [Kouyama & Mihashi (1981) Eur. J. Biochem. 114, 33-38] to monitor pressure-induced relaxations of acto-myosin subfragment 1. This label greatly increases the sensitivity of measurement of dissociated actin and reveals the presence of two relaxations. The experimental data can be fitted by a model in which actin binds subfragment 1 relatively weakly (K = 5.9 × 10(4) M-1) and then isomerizes to a more tightly bound complex (K = 1.7 × 10(7) M-1). This directly observed isomerization supports the model of Geeves, Goody & Gutfreund [(1984) J. Muscle Res. Cell. Motil. 5, 351-361]. The rate of the isomerization is too high to be observed in the pressure-jump apparatus (less than 200 microseconds), but analysis of the amplitudes allows estimation of the equilibrium constant of the isomerization as 280 (20 degrees C, 0.1 M-KCl, pH 7). The equilibrium is sensitive to temperature, pressure, ionic strength and the presence of ethylene ...

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Sheep polyclonal fast skeletal Myosin antibody validated for WB, IP, ELISA, IHC, Neut, ICC/IF and tested in Human, Mouse, Rat and Rabbit. Immunogen…

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- Conference Call Today at 4:30 p.m. EST PASADENA, Calif.--(BUSINESS WIRE)-- Arrowhead Research Corporation (NASDAQ...

- Conference Call Today at 4:30 p.m. EDT PASADENA, Calif.--(BUSINESS WIRE)-- Arrowhead Research Corporation (NASDAQ...

Antibodies with epitopes near the heavy meromyosin/light meromyosin junction distinguish the folded from the extended conformational states of smooth muscle myosin. Antibody 10S.1 has 100-fold higher avidity for folded than for extended myosin, while antibody S2.2 binds preferentially to the extended state. The properties of these antibodies provide direct evidence that the conformation of the rod is different in the folded than the extended monomeric state, and suggest that this perturbation may extend into the subfragment 2 region of the rod. Two antihead antibodies with epitopes on the heavy chain map at or near the head/rod junction. Magnesium greatly enhances the binding of these antibodies to myosin, showing that the conformation of the heavy chain in the neck region changes upon divalent cation binding to the regulatory light chain. Myosin assembly is also altered by antibody binding. Antibodies that bind to the central region of the rod block disassembly of filaments upon MgATP addition. ...

Using optical trapping and fluorescence imaging techniques, we measured the step size and stiffness of single skeletal myosins interacting with actin filaments and arranged on myosin-rod cofilaments that approximate myosin mechanics during muscle contraction. Stiffness is dramatically lower for negatively compared to positively strained myosins, consistent with buckling of myosins subfragment 2 rod domain. Low stiffness minimizes drag of negatively strained myosins during contraction at loaded conditions. Myosins elastic portion is stretched during active force generation, reducing apparent step size with increasing load, even though the working stroke is approximately constant at about 8 nanometers. Taking account of the nonlinear nature of myosin elasticity is essential to relate myosins internal structural changes to physiological force generation and filament sliding.. ...

Dive into the research topics of Effect of ionic strength on the conformation of myosin subfragment 1-nucleotide complexes. Together they form a unique fingerprint. ...

Fluorescein-labeled heavy meromyosin subfragment-1 (F-S-1) has been purified by ion exchange chromatography and characterized in terms of its ability to bind specifically to actin. F-S-1 activates the Mg++-adenosine triphosphatase activity of rabbit skeletal muscle actin and decorates actin as shown by negative stains and thin sections of rabbit actin and rat embryo cell microfilament bundles, respectively. Binding of F-S-1 to cellular structures is prevented by pyrophosphate and by competition with excess unlabeled S-1. The F-S-1 is used in light microscope studies to determine the distribution of actin-containing structures in wnterphase and mitotic rat embryo and rat kangaroo cells. Interphase cells display the familiar pattern of fluorescent stress fibers. Chromosome-to-pole fibers are fluorescent in mitotic cells. The glycerol extraction procedures employed provide an opportunity to examine cells prepared in an identical manner by light and electron microscopy. The latter technique reveals ...

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This antibody can be used for the study of muscles and their development, including studies of myogenesis. This particular antibody

We used light scattering and ultracentrifugation to study the binding ratio of myosin and actin from normal and failing dog hearts and to determine the effect of temperature and adenosine triphosphate (ATP) on the binding. For comparison, similar studies were done on myosin and actin from rabbit skeletal muscle.. We found a higher combining ratio, by weight, for cardiac myosin and actin (4.8 : 1) than for skeletal myosin and actin (4.4 : 1). The dissociation constants were similar at 24°C for cardiac and skeletal proteins. But at 10°C, the dissociation constant was greater for cardiac proteins, and the difference appeared more pronounced when phosphate was used to buffer the solutions.. The dissociation constant at 10°C was greater for myosin and actin from failing dog hearts.. ATP caused dissociation of cardiac and skeletal F-acto-heavy meromyosin and F-actomyosin. There was evidence that the binding of cardiac proteins may not be as tight as that of skeletal muscle proteins.. ...

Purification of native myosin filaments from muscle.: Analysis of the structure and function of native thick (myosin-containing) filaments of muscle has been ha

The synthesis of [2-3H]ATP with specific activity high enough to use for 3H NMR spectroscopy at micromolar concentrations was accomplished by tritiodehalog

Slow Skeletal Myosin Heavy chain小鼠单克隆抗体[NOQ7.5.4D](ab11083)可与小鼠, 大鼠, 羊, 兔, 山羊, 鸡, 豚鼠, 仓鼠等样本反应并经WB, ELISA, IHC, RIA, EM…

Slow Skeletal Myosin Heavy chain小鼠单克隆抗体可与小鼠, 大鼠, 鸡, 人样本反应并经WB, ELISA, IHC, ICC/IF实验严格验证，被1篇文献引用。

Animals were immunized with partially purified human fetal (15 weeks gestation) skeletal muscle myosin heavy chain. Spleen cells were fused with P3X63Ag8.653 mouse myeloma cells.

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myosin filament packing Sequence divergence of coiled coils--structural rodss profile, publications, research topics, and co-authors

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Analysts expect Arrowhead Pharmaceuticals, Inc. (NASDAQ:ARWR) to report $-0.15 EPS on February, 5.They anticipate $0.02 EPS change or 11.76 % from last

Visualization of the M2 duration HMM. The top WebLogos illustrate nucleotide frequencies in each of the hexamer positions. The bottom WebLogos convert the frequ

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Familial hypertrophic cardiomyopathy (HCM) is caused by mutations in 9 sarcomeric protein genes. The most commonly affected is beta-myosin heavy chain (MYH7), where missense mutations cluster in the head and neck regions and directly affect motor function. Comparable mutations have not been described in the light meromyosin (LMM) region of the myosin rod, nor would these be expected to directly affect motor function. We studied 82 probands with HCM in whom no mutations had been found in MYH7 exons encoding the head and neck regions of myosin nor in the other frequently implicated disease genes. Primers were designed to amplify exons 24 to 40 of MYH7. These amplimers were subjected to temperature modulated heteroduplex analysis by denaturing high-performance liquid chromatography. An Ala1379Thr missense mutation in exon 30 segregated with disease in three families and was not present in 200 normal chromosomes. The mutation occurred on two haplotypes, indicating that it was not a polymorphism linked with

Muscle contraction involves the interaction of the myosin heads of the thick filaments with actin subunits of the thin filaments. Relaxation occurs when this interaction is blocked by molecular switches on these filaments. In many muscles, myosin-linked regulation involves phosphorylation of the myosin regulatory light chains (RLCs). Electron microscopy of vertebrate smooth muscle myosin molecules (regulated by phosphorylation) has provided insight into the relaxed structure, revealing that myosin is switched off by intramolecular interactions between its two heads, the free head and the blocked head. Three-dimensional reconstruction of frozen-hydrated specimens revealed that this asymmetric head interaction is also present in native thick filaments of tarantula striated muscle. Our goal in this study was to elucidate the structural features of the tarantula filament involved in phosphorylation-based regulation. A new reconstruction revealed intra- and intermolecular myosin interactions in ...

Comments on Hoppe PE et al. (2000) Genetics A region of the myosin rod important for interaction with paramyosin in Caenorhabditis elegans striated muscle. ...

NOTCH proteins constitute a receptor family with a widely conserved role in cell cycle, growing and development regulation. NOTCH1, the best characterised

View Notes - 7 from NPB NPB 101 at UC Davis. 9) Exposed actin sites bind with the myosin heads, which have been previously energized by hydrolysis of ATP at the ATPase 10) Binding of actin and myosin

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Founded in 1920, the NBER is a private, non-profit, non-partisan organization dedicated to conducting economic research and to disseminating research findings among academics, public policy makers, and business professionals.

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ウサギ・ポリクローナル抗体 ab91506 交差種: Ms,Rat,Hu,Pig 適用: WB,IHC-P,IHC-Fr…Fast Myosin Skeletal Heavy chain抗体一覧…画像、プロトコール、文献などWeb上の情報が満載のアブカムの…

The maximum number of securities that will be considered on a Request for LMM Issue Assignment Form will be the number of securities for which the CHX Participant is eligible for LMM issue assignment minus the number of securities for which the CHX Participant has already been assigned as an LMM. If granting a Request for LMM Issue Assignment Form regarding a given security would result in exceeding the cap on LMM issue assignments for that security or would result in the LMM having more than 500 LMM issue assignments (or a larger number already approved by CHX), then CHX shall limit consideration of the Request for LMM Issue Assignment Form to the top number of lines based on the difference between the CHX Participants number of eligible securities for LMM issue assignment and the number already assigned ...

Training notes: practice uke against a post. It allows you to develop the blocks in association with sabaki and stances. It is important to feel resistance against the forearm on the target zones, to feel where the lines intersect, where tangents are made between lines and curves of force. Stay close to the post, stay as close as possible. Push-up/fall-down against the post when doing age-uke, toboku ho, fall against the weight. When doing jodan-age uke, you should feel yourself pushing up against an arm as you fall into your opponent - falling and rising at the same time ...

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Telokin, an abundant gizzard protein, inhibited phosphorylation of regulatory light chain when filamentous myosin was used as the substrate but no inhibition was observed with myosin subfragment 1. At physiological telokin-to-myosin molar ratio (1:1), the inhibition amounted to a 3.5-fold reduction in the initial phosphorylation rate whereas at high molar excess of telokin over myosin, we observed an up to 20-fold decrease in this rate. In agreement with previous observations [Shirinsky, Vorotnikow, Birukov, Nanaev, Collinge, Lukas, Sellers and Watterson (1993) J. Biol. Chem. 268, 16578Ő16583], telokin did not inhibit phosphorylation of the isolated regulatory light chain of myosin and only moderately (35%) inhibited that of heavy meromyosin. To gain a better understanding of the mechanism of this inhibition, we investigated the effects of telokin on the recently described [Babiychuk, Babiychuk and Sobieszek (1995) Biochemistry 34, 6366Ő6372] oligomeric properties of smooth-muscle myosin ...

TY - JOUR. T1 - Analysis of stress in the active site of myosin accompanied by conformational changes in transient state intermediate complexes using photoaffinity labeling and 19F-NMR spectroscopy. AU - Maruta, Shinsaku. AU - Henry, Gillian D.. AU - Ohki, Takashi. AU - Kambara, Taketoshi. AU - Sykes, Brian D.. AU - Ikebe, Mitsuo. PY - 1998/3/15. Y1 - 1998/3/15. N2 - Myosin forms stable ternary complexes with ADP and the phosphate analogues, fluoroaluminate (Al F4/-), fluoroberyllate (BeF(n)) or orthovanadate (Vi); these ternary complexes mimic transient intermediates in the myosin ATPase cycle. Moreover, we previously demonstrated that these complexes may mimic different myosin ATPase reaction intermediates corresponding to separate steps in the cross-bridge cycle [Maruta, S., Henry, G. D., Sykes, B. D. and Ikebe, M. (1993) J. Biol. Chem. 268, 7093-7100]. Park et al. suggested that the changing conformation of ATP during hydrolysis stresses the active site of myosin subfragment-1 (S-1) through ...

MYH7 is a gene encoding a myosin heavy chain beta (MHC-β) isoform (slow twitch) expressed primarily in the heart, but also in skeletal muscles (type I fibers). This isoform is distinct from the fast isoform of cardiac myosin heavy chain, MYH6, referred to as MHC-α. MHC-β is the major protein comprising the thick filament in cardiac muscle and plays a major role in cardiac muscle contraction. MHC-β is a 223 kDa protein composed of 1935 amino acids. MHC-β is a hexameric, asymmetric motor forming the bulk of the thick filament in cardiac muscle. MHC-β is composed of N-terminal globular heads (20 nm) that project laterally, and alpha helical tails (130 nm) that dimerize and multimerize into a coiled-coil motif to form the light meromyosin (LMM), thick filament rod. The 9 nm alpha-helical neck region of each MHC-β head non-covalently binds two light chains, essential light chain (MYL3) and regulatory light chain (MYL2). Approximately 300 myosin molecules constitute one thick filament. There ...

TY - JOUR. T1 - High-performance ion-exchange chromatography of myosin using a DEAE-5PW column. AU - Lema, Mark J.. AU - Pluskal, Malcolm G.. AU - Allen, Paul D.. PY - 1989. Y1 - 1989. N2 - High-performance ion-exchange chromatography of myosin using a DEAE-5PW packing was used to purify myosin from skeletal, cardiac and smooth muscle. This method produces high-speed resolution (30-min analysis) of myosin from contaminating myofibrillar proteins. The column has a high capacity for binding myosin (up to 1 g) and can be used for small-scale preparation of highly purified myosin. Gel analysis in the presence of sodium dodecyl sulfate showed recovery of myosin with very little contamination of other myofibrillar proteins. Myosin was also recovered from small biopsy samples (0.1 g) by a direct extraction technique with recovery of biological ATPase activity.. AB - High-performance ion-exchange chromatography of myosin using a DEAE-5PW packing was used to purify myosin from skeletal, cardiac and ...

1B7T|br|MYOSIN DIGESTED BY PAPAIN|br|DOI: 10.2210/pdb1b7t/pdb|br|Classification: MYOSIN|br|Deposited: 1999-01-15 Released: 1999-05-12|br|Deposition author(s): Houdusse, A., Kalabokis, V., Himmel, D., Szent-|br|Gyorgyi, A.G., Cohen, C.|br|Organism: Argopecten irradians|br|Structural Biology Knowledgebase: 1B7T (15 models >15 annotations) |br|SBKB.org|br|Experimental Data Snapshot|br|Method: X-RAY DIFFRACTION|br|Resolution: 2.5 Å|br|R-Value Free: 0.297|br|R-Value Work: 0.224|br|wwPDB Validation Full Report|br|Primary Citation |br|Atomic structure of scallop myosin subfragment S1 complexed with MgADP: a novel conformation of the myosin head.|br|Houdusse, A., Kalabokis, V.N., Himmel, D., Szent-Gyorgyi, A.G., Cohen, C.|br|(1999) Cell(Cambridge,Mass.) 97: 459-470|br|http://www.rcsb.org/pdb/explore/explore.do?structureId=1B7T

Arrowhead Pharmaceuticals Inc. (NASDAQ: ARWR) today announced that it is scheduled to participate in the following upcoming events: 2019 Cantor Global Healthcare Conference - New York, October 2-4, 2019 October 4, 10:05 a.m. EDT - Vince Anzalone, CFA, Arrowheads vice president of investor relations, will participate in a fireside chat presentation with Elemer Piros, Ph.D., Cantor Fitzgerald biotechnology equity research analyst Chardan 3rd Annual Genetic Medicines Conference - New York, October 7-8, 2019 October 7, 1:30 p.m. EDT - Bruce Given, M.D., Arrowheads chief operating officer and head of R&D, will participate in a fireside chat presentation with Keay Nakae, CFA, Chardan senior research analyst Arrowhead Pharmaceuticals Analyst R&D Day - New York, October 18, 2019 October 18, 8:30-11:30 a.m. EDT - Arrowhead and outside experts will provide updates on the companys emerging pipeline of RNAi therapeutics and review advancements being made to the proprietary Targeted RNAi Molecule (TRiMTM) ...

Mouse monoclonal antibody raised against native myosin heavy chain (fast). Native Myosin Heavy Chain (fast) from rabbit psoas muscle. (MAB9512) - Products - Abnova

Arrowhead Pharmaceuticals, Inc.(ARWR): For the most recent quarter end, Arrowhead Pharmaceuticals, Inc. reported Annual Earnings of $-0.17. Based on the filings, last years Annual Earnings was, $-1.31. For the most recent quarter end, ARWR reported a surprise Earnings per Share of 5.56% . The consensus estimate for current quarter is $-0.12 and for the current fiscal year, the estimate is $-0.49. For the Next fiscal year, the estimate is $-0.66 based on the consensus. Pasadena based Arrowhead Pharmaceuticals, Inc. Last reported the Quarter results on Dec 31, 2016 and the Next earnings date is scheduled to be released on May 09, 2017. Arrowhead Pharmaceuticals, Inc. has received $-0.12 as the consensus Earnings Estimate for the Quarter ending on Mar 2017 ,According to the estimate provided by 3 Financial Advisor in the Stock Trading Firms. Among 3 Analysts, Bottom line EPS Estimate for the current quarter is $-0.16 while the top line estimate is $-0.1 , a key information to consider for Day ...

TY - JOUR. T1 - Two-dimensional arrangement of a functional protein by cysteine-gold interaction. T2 - Enzyme activity and characterization of a protein monolayer on a gold substrate. AU - Sasaki, Yuji C.. AU - Yasuda, Kenji. AU - Suzuki, Yoshio. AU - Ishibashi, Tadashi. AU - Satoh, Isamu. AU - Fujiki, Yasutake. AU - Ishiwata, Shinichi. PY - 1997/4. Y1 - 1997/4. N2 - We have characterized the functional protein, myosin subfragment 1 (S1), attached to a gold substrate by the sulfhydryl groups of cysteine in proteins. The amino groups of the regulatory light chain (RLC) isolated from myosin were labeled with a radioisotope (125I), and the labeled RLC was incorporated into S1 from which the RLC had been removed. The radiation from 125I showed that S1 molecules had attached to the gold and, through the interference effect of the monochromatic radiation from 125I, provided information about the position of labeled RLC sites in the S1 monolayer. The interference fringes showed that the RLC was ...

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A myosin complex containing one or more class XVII myosin heavy chains and associated light chains. [http://www.mrc-lmb.cam.ac.uk/myosin/Review/Reviewframeset.html]

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1KK7: Crystallographic findings on the internally uncoupled and near-rigor states of myosin: further insights into the mechanics of the motor.

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@TTraw said in What if we removed 1 card per category?: Hmm, Id say this are some of the ones Id defend the most (I didnt consider those that you proposed to move or merge, that would be a different discussion): Equivalent Exchange (Q): Heal for {10...