PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 8373821-0 1993 The ATP-induced myosin subfragment-1 fluorescence intensity increase is due to one tryptophan. Tryptophan 83-93 myosin heavy chain 14 Homo sapiens 16-22 8341700-1 1993 A well-known indication that a nucleotide has bound to myosin is the enhancement of the fluorescence of a specific tryptophan in the "subfragment 1" segment of the protein. Tryptophan 115-125 myosin heavy chain 14 Homo sapiens 55-61 1390932-1 1992 The effects of nucleotide binding and temperature on the internal structural dynamics of myosin subfragment 1 (S1) were monitored by intrinsic tryptophan phosphorescence lifetime and fluorescence anisotropy measurements. Tryptophan 143-153 myosin heavy chain 14 Homo sapiens 89-95 3593699-5 1987 U.S.A. 76, 3382-3386] cross-links two [50 and 20 kilodaltons (kDa)] of the three major fragments of myosin subfragment 1 (S-1); on intact S-1, DBB quenches tryptophans and inhibits all ATPases [Mornet, D., Ue, K., & Morales, M. F. (1985) Proc. Tryptophan 156-167 myosin heavy chain 14 Homo sapiens 100-106 2207184-1 1990 Thermal denaturation of myosin rod has been studied by differential scanning microcalorimetry and intrinsic tryptophane fluorescence methods. Tryptophan 108-119 myosin heavy chain 14 Homo sapiens 24-30 2207184-3 1990 Changes of the time resolved and steady state fluorescence of myosin rod were interpreted using the data on localization of tryptophan residues in the molecule. Tryptophan 124-134 myosin heavy chain 14 Homo sapiens 62-68 2207184-4 1990 The tryptophan fluorescence of myosin rod is assumed to monitor the denaturational changes in high meromyosin and probably in the hinge region but not in the subfragment 2. Tryptophan 4-14 myosin heavy chain 14 Homo sapiens 31-37 3167066-2 1988 The changes in actin structure under the influence of these regulatory complexes, as well as those upon the binding of the myosin heads, were followed by measurements of F-actin intrinsic tryptophan fluorescence and the fluorescence of phalloidin-rhodamine complex attached to F-actin. Tryptophan 188-198 myosin heavy chain 14 Homo sapiens 123-129 3606998-0 1987 Modification of myosin subfragment 1 tryptophans by dimethyl(2-hydroxy-5-nitrobenzyl)sulfonium bromide. Tryptophan 37-48 myosin heavy chain 14 Homo sapiens 16-22 6223922-5 1983 According to the theory of polarization of the fluorescence of proteins, it is likely that some tryptophan residues of myosin, which are responsible for the increase in the fluorescence intensity and polarization when myosin interacts with substrates, reduce their local freedom of rotation. Tryptophan 96-106 myosin heavy chain 14 Homo sapiens 119-125 6223922-5 1983 According to the theory of polarization of the fluorescence of proteins, it is likely that some tryptophan residues of myosin, which are responsible for the increase in the fluorescence intensity and polarization when myosin interacts with substrates, reduce their local freedom of rotation. Tryptophan 96-106 myosin heavy chain 14 Homo sapiens 218-224 6895374-1 1981 The interaction of calmodulin with myosin light chain kinase produces an approximately 30% increase in myosin light chain kinase tryptophan fluorescence. Tryptophan 129-139 myosin heavy chain 14 Homo sapiens 35-41 6951179-7 1982 In contrast, the MgATP-induced increase in tryptophan fluorescence of myosin subfragment 1 appeared without a lag phase. Tryptophan 43-53 myosin heavy chain 14 Homo sapiens 70-76 7013787-0 1981 Environment of the tryptophan residues in a myosin head: a hydrogen-deuterium exchange study. Tryptophan 19-29 myosin heavy chain 14 Homo sapiens 44-50 12741846-2 2003 Myosin"s conserved ATP-sensitive tryptophan (AST) is an energy transduction optical sensor signaling transduction-related transient conformation change by modulating its fluorescence intensity amplitude and relaxation rate. Tryptophan 33-43 myosin heavy chain 14 Homo sapiens 0-6 1214799-2 1975 Analysis of the experimental results of myosin fluorescence quenching with I-ions and the quantum yield of the fluorescence at the excitation wavelength 296 nm shows that the greater part of the tryptophan residues (21 out of 28) is located in the hydrophylic environment. Tryptophan 195-205 myosin heavy chain 14 Homo sapiens 40-46 21212073-5 2011 In contrast, during MANTTP hydrolysis, significant fluorescence resonance energy transfer (FRET) was observed between MANTTP and intrinsic tryptophan residues in the myosin motor domain. Tryptophan 139-149 myosin heavy chain 14 Homo sapiens 166-172 18211892-3 2008 To investigate the binding and the release of ADP and phosphate independently from the lever arm motion, two single tryptophan-containing motor domains of Dictyostelium myosin II were used. Tryptophan 116-126 myosin heavy chain 14 Homo sapiens 169-175 17913331-5 2007 The trajectory shows myosin transduction of free energy to mechanical work giving evidence for: (i) a causal relationship between product release and work production in the native isoform that is correctly disrupted in a chemically modified protein, (ii) the molecular basis of ATP-sensitive tryptophan fluorescence enhancement and acrylamide quenching, (iii) an actin-binding site peptide containing the free-energy barrier to ATPase product release defining the rate limiting step and, (iv) a scenario for actin-activation of myosin ATPase. Tryptophan 292-302 myosin heavy chain 14 Homo sapiens 21-27 17913331-5 2007 The trajectory shows myosin transduction of free energy to mechanical work giving evidence for: (i) a causal relationship between product release and work production in the native isoform that is correctly disrupted in a chemically modified protein, (ii) the molecular basis of ATP-sensitive tryptophan fluorescence enhancement and acrylamide quenching, (iii) an actin-binding site peptide containing the free-energy barrier to ATPase product release defining the rate limiting step and, (iv) a scenario for actin-activation of myosin ATPase. Tryptophan 292-302 myosin heavy chain 14 Homo sapiens 528-534 17704147-4 2007 Fluorescence increase in the nucleotide sensitive tryptophan (NST) accompanies nucleotide binding and hydrolysis in several myosin isoforms implying it results from a common origin within the motor. Tryptophan 50-60 myosin heavy chain 14 Homo sapiens 124-130 17640901-6 2007 Overall, state change seems to occur by attachment of a hydrophobic triplet (Trp-546, Phe-547, and Pro-548) of myosin to an actin conduit with a hydrophobic guiding rail (Ile-341, Ile-345, Leu-349, and Phe-352) and the subsequent linear movement of the triplet along the rail. Tryptophan 77-80 myosin heavy chain 14 Homo sapiens 111-117 15351647-7 2004 According to crystallographic and tryptophan fluorescence studies, all of these analogs, except ATPgammaS and ADP, induce the "closed" conformation of the myosin head (in which the gamma phosphate pocket is closed). Tryptophan 34-44 myosin heavy chain 14 Homo sapiens 155-161 432955-0 1979 [Nature of the orientation of the tryptophan residues in the myosin and actin from striated muscle fiber]. Tryptophan 34-44 myosin heavy chain 14 Homo sapiens 61-67 432955-1 1979 The mode of tryptophan residue orientation in myosin and action myofilaments of the muscle fiber was studied using polarized ultraviolet (UV) fluorescent microscopy of the muscle fiber was studied using polarized ultraviolet (UV) fluorescent microscopy technique. Tryptophan 12-22 myosin heavy chain 14 Homo sapiens 46-52 21536675-5 2011 Here we use single tryptophan mutants of smooth muscle myosin to determine how conformational changes in switch I are correlated with structural changes in the nucleotide and actin-binding clefts in the presence of actin and ADP. Tryptophan 19-29 myosin heavy chain 14 Homo sapiens 55-61 17449872-3 2007 By introducing point mutations into a subdomain interface at the base of the myosin lever arm at positions Lys(84) and Arg(704), we caused modulatory changes in the equilibrium constant of the recovery stroke, which we could accurately resolve using the fluorescence signal of single tryptophan Dictyostelium myosin II constructs. Tryptophan 284-294 myosin heavy chain 14 Homo sapiens 77-83 17449872-3 2007 By introducing point mutations into a subdomain interface at the base of the myosin lever arm at positions Lys(84) and Arg(704), we caused modulatory changes in the equilibrium constant of the recovery stroke, which we could accurately resolve using the fluorescence signal of single tryptophan Dictyostelium myosin II constructs. Tryptophan 284-294 myosin heavy chain 14 Homo sapiens 309-315 17213877-3 2007 Single tryptophan residues were introduced into the switch 1 region of myosin II motor domain and studied by rapid reaction methods. Tryptophan 7-17 myosin heavy chain 14 Homo sapiens 71-77 15699387-3 2005 The authors have identified the arginine 1845 tryptophan mutation found in the Swedish families in two isolated Belgian cases, indicating a critical role for myosin residue arginine 1845. Tryptophan 46-56 myosin heavy chain 14 Homo sapiens 158-164 11123942-0 2000 Resolution of conformational states of Dictyostelium myosin II motor domain using tryptophan (W501) mutants: implications for the open-closed transition identified by crystallography. Tryptophan 82-92 myosin heavy chain 14 Homo sapiens 53-59 11959853-3 2002 Steady-state fluorescence of F425W-MDE demonstrates that Trp-425 is in a more solvent-exposed conformation in the presence of MgATP than in the presence of MgADP or absence of nucleotide, consistent with closure of the actin-binding cleft in the strongly bound states of MgATPase cycle for myosin. Tryptophan 57-60 myosin heavy chain 14 Homo sapiens 290-296 11959853-4 2002 Transient kinetic experiments demonstrate a direct correlation between the rates of strong actin binding and the conformation of Trp-425 in the actin-binding cleft, and suggest the existence of a novel conformation of myosin not previously seen in solution or by x-ray crystallography. Tryptophan 129-132 myosin heavy chain 14 Homo sapiens 218-224 11904418-6 2002 We found that the Arg-719 --> Trp (Arg719Trp) mutation, which is located in the converter domain of the myosin head fragment, causes an increase in force generation and fiber stiffness under isometric conditions by 48-59%. Tryptophan 33-36 myosin heavy chain 14 Homo sapiens 107-113 11170382-8 2001 In this framework, we suggest that (1) in the actin-myosin association phase, cationic residues Lys-576 and Lys-578 interact with anionic residues of the so-called second actin, and (2) in the product leaving phase, hydrophobic residues Trp-546, Phe-547, and Pro-548, as well as the Thr-532/Asn-533/Pro-534/Pro-535 sequence, sever connections with the so-called first actin. Tryptophan 237-240 myosin heavy chain 14 Homo sapiens 52-58 12429851-7 2002 From the behavior of recombinant myosin systems in which Arg-247 and Glu-470 were substituted in several ways, we draw the conclusions that (i) the force between Arg-247 and gamma-phosphate of ATP may assist in closing the cleft, and incidentally in signaling to the remote Trp, and (ii) in catalysis, Glu-470 is involved in holding the lytic H(2)O (w(1)). Tryptophan 274-277 myosin heavy chain 14 Homo sapiens 33-39 11971905-0 2002 Analysis of nucleotide binding to Dictyostelium myosin II motor domains containing a single tryptophan near the active site. Tryptophan 92-102 myosin heavy chain 14 Homo sapiens 48-54 11971905-6 2002 Overall, we conclude that the local and global conformational changes in myosin IIs induced by nucleotide binding are similar in myosins from different species, but the sign and magnitude of the tryptophan fluorescence changes reflect nonconserved residues in the immediate vicinity of each tryptophan. Tryptophan 195-205 myosin heavy chain 14 Homo sapiens 73-79 11971905-6 2002 Overall, we conclude that the local and global conformational changes in myosin IIs induced by nucleotide binding are similar in myosins from different species, but the sign and magnitude of the tryptophan fluorescence changes reflect nonconserved residues in the immediate vicinity of each tryptophan. Tryptophan 291-301 myosin heavy chain 14 Homo sapiens 73-79 11123942-1 2000 When myosin interacts with ATP there is a characteristic enhancement in tryptophan fluorescence which has been widely exploited in kinetic studies. Tryptophan 72-82 myosin heavy chain 14 Homo sapiens 5-11 10827189-0 2000 Tryptophan 512 is sensitive to conformational changes in the rigid relay loop of smooth muscle myosin during the MgATPase cycle. Tryptophan 0-10 myosin heavy chain 14 Homo sapiens 95-101 10827189-3 2000 Thus, Trp-512 may be the sole ATP-sensitive tryptophan residue in myosin. Tryptophan 6-9 myosin heavy chain 14 Homo sapiens 66-72 10827189-3 2000 Thus, Trp-512 may be the sole ATP-sensitive tryptophan residue in myosin. Tryptophan 44-54 myosin heavy chain 14 Homo sapiens 66-72 10827189-6 2000 We conclude that the conformation of the rigid relay loop containing Trp-512 is altered upon MgATP hydrolysis and during the transition from weak to strong actin binding, establishing a communication pathway from the active site to the actin-binding and converter/lever arm regions of myosin during muscle contraction. Tryptophan 69-72 myosin heavy chain 14 Homo sapiens 285-291 10820029-2 2000 In human beta-cardiac myosin, mutation of arginine-403 to a glutamine or a tryptophan causes hypertrophic cardiomyopathy. Tryptophan 75-85 myosin heavy chain 14 Homo sapiens 22-28 7548005-7 1995 Xestoquinone modified myosin SH groups which caused changes in the tryptophan fluorescence intensity and circular dichroism. Tryptophan 67-77 myosin heavy chain 14 Homo sapiens 22-28 9860965-2 1998 To monitor this change, we have measured distances between a gizzard regulatory light chain (Cys 108) and the active site (near or at Trp 130) of skeletal myosin subfragment 1 (S1) by using luminescence resonance energy transfer and a photoaffinity ATP-lanthanide analog. Tryptophan 134-137 myosin heavy chain 14 Homo sapiens 155-161 9500922-1 1998 Light meromyosin (LMM 77), the C-terminal proteolytic peptide from myosin rod, is a 900 A coiled-coil that contains two pairs of tryptophan residues in d-positions of the heptad repeat (abcdefg)n. Previous studies showed that LMM 77 unfolded in two transitions and suggested that both Trp pairs were located in the least stable unfolding domain. Tryptophan 129-139 myosin heavy chain 14 Homo sapiens 10-16 9500922-1 1998 Light meromyosin (LMM 77), the C-terminal proteolytic peptide from myosin rod, is a 900 A coiled-coil that contains two pairs of tryptophan residues in d-positions of the heptad repeat (abcdefg)n. Previous studies showed that LMM 77 unfolded in two transitions and suggested that both Trp pairs were located in the least stable unfolding domain. Tryptophan 285-288 myosin heavy chain 14 Homo sapiens 10-16 8981751-1 1996 The xanthene probes 5"-iodoacetamido-fluorescein and -tetramethylrhodamine specifically modify skeletal muscle myosin subfragment 1 (S1) at the reactive thiol residue (SH1) and fully quench the fluorescence emission from tryptophan residue 510 (Trp510) in S1 (T.P. Tryptophan 221-231 myosin heavy chain 14 Homo sapiens 111-117 8765220-1 1996 The probe binding cleft of myosin subfragment 1 (S1) contains the reactive thiol, SH1, and tryptophan 510 (Trp-510). Tryptophan 91-101 myosin heavy chain 14 Homo sapiens 27-33 8765220-1 1996 The probe binding cleft of myosin subfragment 1 (S1) contains the reactive thiol, SH1, and tryptophan 510 (Trp-510). Tryptophan 107-110 myosin heavy chain 14 Homo sapiens 27-33 8981751-0 1996 Optical activity of a nucleotide-sensitive tryptophan in myosin subfragment 1 during ATP hydrolysis. Tryptophan 43-53 myosin heavy chain 14 Homo sapiens 57-63 8536695-5 1995 At alkaline pH, the fluorescence of the myosin rod was quenched, and the tryptophan region of the protein became less stable in the presence of guanidine hydrochloride, due to ionization of tyrosine residues or other amino acids close to tryptophans in the double-helix arrangement. Tryptophan 238-249 myosin heavy chain 14 Homo sapiens 40-46