PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 8003981-0 1994 Distribution of distances between the tryptophan and the N-terminal residue of melittin in its complex with calmodulin, troponin C, and phospholipids. Tryptophan 38-48 calmodulin 1 Homo sapiens 108-118 7935351-4 1993 Binding stoichiometry and affinity were determined by following the enhancement in tryptophane fluorescence occurring upon 1:1 complex formation between these peptides and calmodulin. Tryptophan 83-94 calmodulin 1 Homo sapiens 172-182 8299556-7 1994 Treatment of the cells with the calmodulin antagonist CGS 9343 B stimulated the uptake of leucine and tryptophan, but inhibited the uptake of T3. Tryptophan 102-112 calmodulin 1 Homo sapiens 32-42 24242906-1 1991 An engineered calmodulin (VU-9-CaM) has been prepared in which a tryptophan group is present at position 99 and a tyrosine at position 138. Tryptophan 65-75 calmodulin 1 Homo sapiens 14-24 24234718-2 1993 Calmodulin has no tryptophan residues but possesses two tyrosines (at positions 99 and 138) in the C-terminal half of the protein. Tryptophan 18-28 calmodulin 1 Homo sapiens 0-10 1790714-8 1991 However, when mixed with CaM the Pep C undergoes both a dramatic blue-shift in tryptophan fluorescence emission, indicative of strong hydrophobic interaction, and an increase in circular dichroism absorption in the alpha-helical region. Tryptophan 79-89 calmodulin 1 Homo sapiens 25-28 1854758-0 1991 Fluorescence analysis of calmodulin mutants containing tryptophan: conformational changes induced by calmodulin-binding peptides from myosin light chain kinase and protein kinase II. Tryptophan 55-65 calmodulin 1 Homo sapiens 25-35 1854758-0 1991 Fluorescence analysis of calmodulin mutants containing tryptophan: conformational changes induced by calmodulin-binding peptides from myosin light chain kinase and protein kinase II. Tryptophan 55-65 calmodulin 1 Homo sapiens 101-111 1854758-10 1991 Both peptides induced similar changes in the fluorescence properties of the tryptophan residues located in the calcium-binding loops, with the exception of calmodulin with Trp-135. Tryptophan 172-175 calmodulin 1 Homo sapiens 156-166 1854758-15 1991 These results provide evidence that the environment of Trp-81 is different in each case and are, therefore, consistent with the hypothesis that the central helix can play a differential role in the recognition of, or response to, CaM-binding structures. Tryptophan 55-58 calmodulin 1 Homo sapiens 230-233 2526124-5 1989 Substituting tyrosine (C28Y) or alanine (C28A) for the tryptophan residue lowered the affinity for calmodulin. Tryptophan 55-65 calmodulin 1 Homo sapiens 99-109 2154244-7 1990 A tryptophan that is conserved in most calmodulin binding domains of proteins was replaced by other amino acids, giving rise to modified peptides which had lower affinity for calmodulin. Tryptophan 2-12 calmodulin 1 Homo sapiens 39-49 2154244-7 1990 A tryptophan that is conserved in most calmodulin binding domains of proteins was replaced by other amino acids, giving rise to modified peptides which had lower affinity for calmodulin. Tryptophan 2-12 calmodulin 1 Homo sapiens 175-185 3196313-2 1988 Addition of calmodulin to caldesmon causes a concentration-dependent shortwave shift and an increase of fluorescence intensity of caldesmon tryptophan residues. Tryptophan 140-150 calmodulin 1 Homo sapiens 12-22 2622908-8 1989 After photocross-linking the Bpa residue of this peptide to Met-71 of calmodulin, it could be shown that the fluorescence properties of the Trp residue were consistent with its side chain being buried in a hydrophobic pocket on the C-terminal domain of calmodulin. Tryptophan 140-143 calmodulin 1 Homo sapiens 70-80 2622908-8 1989 After photocross-linking the Bpa residue of this peptide to Met-71 of calmodulin, it could be shown that the fluorescence properties of the Trp residue were consistent with its side chain being buried in a hydrophobic pocket on the C-terminal domain of calmodulin. Tryptophan 140-143 calmodulin 1 Homo sapiens 253-263 3182830-2 1988 A mutant calmodulin, in which phenylalanine 99 of calcium binding site III was changed to a tryptophan by using cassette-based, site-directed mutagenesis, has been used to analyze the mechanism of calcium binding. Tryptophan 92-102 calmodulin 1 Homo sapiens 9-19 3182830-3 1988 The combined study of direct calcium binding, modification of tryptophan fluorescence properties upon calcium binding, and terbium titration allows some discrimination among proposed mechanisms of cation binding to calmodulin. Tryptophan 62-72 calmodulin 1 Homo sapiens 215-225 2844821-7 1988 It is concluded that Ser-Lys-Thr-Ala-Ser-Pro-Trp-Lys-Ser-Ala-Arg-Leu-Met-Val-His-Thr-Val-Ala- Thr- Phe-Asn-Ser-Ile-Lys, a 24-residue peptide which bridges repeats 11 and 12 of brain alpha spectrin contains the high affinity calmodulin binding domain. Tryptophan 45-48 calmodulin 1 Homo sapiens 224-234 2775753-0 1989 Fluorescence characterization of VU-9 calmodulin, an engineered calmodulin with one tryptophan in calcium binding domain III. Tryptophan 84-94 calmodulin 1 Homo sapiens 38-48 2775753-2 1989 Tryptophan 99 fluoresces with a maximum around 348 nm and is easily quenched by fluorescence quenchers such as acrylamide, indicating that the chromophore is in a polar environment and well exposed to the solvent, a location which has been reported previously for tyrosine 99 in mammalian calmodulin [Kilhoffer, M. C., Demaille, J. G., & Gerard, D. (1981) Biochemistry 20, 4407-4414]. Tryptophan 0-10 calmodulin 1 Homo sapiens 289-299 2775754-0 1989 Time-resolved fluorescence study of VU-9 calmodulin, an engineered calmodulin possessing a single tryptophan residue. Tryptophan 98-108 calmodulin 1 Homo sapiens 41-51 2775754-0 1989 Time-resolved fluorescence study of VU-9 calmodulin, an engineered calmodulin possessing a single tryptophan residue. Tryptophan 98-108 calmodulin 1 Homo sapiens 67-77 2775754-1 1989 An engineered calmodulin (VU-9 calmodulin), which possesses a single tryptophan residue at position 99 in calcium binding domain III, was studied by time-resolved fluorescence. Tryptophan 69-79 calmodulin 1 Homo sapiens 14-24 2775754-1 1989 An engineered calmodulin (VU-9 calmodulin), which possesses a single tryptophan residue at position 99 in calcium binding domain III, was studied by time-resolved fluorescence. Tryptophan 69-79 calmodulin 1 Homo sapiens 31-41 3196313-4 1988 These findings allow application of the method of protein intrinsic tryptophan fluorescence for quantitative study of unmodified caldesmon and calmodulin in solution. Tryptophan 68-78 calmodulin 1 Homo sapiens 143-153 3196313-8 1988 The results obtained suggest that caldesmon tryptophan residues, together with charged groups, are involved in calmodulin binding. Tryptophan 44-54 calmodulin 1 Homo sapiens 111-121 3219335-2 1988 CaM 78-148 exhibited Ca2+-dependent binding to mastoparan X, Polistes mastoparan, and melittin with apparent dissociation constants less than 0.2 microM as judged from changes in the fluorescence spectrum and anisotropy of the single tryptophan residue of each of these cationic, amphiphilic peptides. Tryptophan 234-244 calmodulin 1 Homo sapiens 0-3 3219335-6 1988 The binding of the peptide to CaM 78-148 also caused a significant loss of the accessibility of the peptide tryptophan to the fluorescence quencher acrylamide. Tryptophan 108-118 calmodulin 1 Homo sapiens 30-33 3219335-7 1988 The CaM 78-148 induced effects on the fluorescence spectra and tryptophan accessibility of the peptides were most pronounced for mastoparan X, a peptide with tryptophan on the apolar face of the putative amphiphilic helix. Tryptophan 63-73 calmodulin 1 Homo sapiens 4-7 3219335-7 1988 The CaM 78-148 induced effects on the fluorescence spectra and tryptophan accessibility of the peptides were most pronounced for mastoparan X, a peptide with tryptophan on the apolar face of the putative amphiphilic helix. Tryptophan 158-168 calmodulin 1 Homo sapiens 4-7 3395656-8 1988 Energy transfer from tryptophan to a pyridoxamine derivatized side group in RNase increased 40% over 25 degrees C. Here we report further testing of this model in two additional protein systems: calmodulin, a calcium activated regulatory protein, and transferrin, a blood serum iron shuttle. Tryptophan 21-31 calmodulin 1 Homo sapiens 195-205 2967288-8 1988 Addition of CaM to FP57-Trp increased peptide tryptophanyl fluorescence. Tryptophan 24-27 calmodulin 1 Homo sapiens 12-15 2967288-9 1988 In the presence of Ca2+, the stoichiometry of the FP57-Trp.CaM complex was 1:1, FP57-Trp binding to CaM was competitive with neuromodulin. Tryptophan 55-58 calmodulin 1 Homo sapiens 59-62 2967288-9 1988 In the presence of Ca2+, the stoichiometry of the FP57-Trp.CaM complex was 1:1, FP57-Trp binding to CaM was competitive with neuromodulin. Tryptophan 55-58 calmodulin 1 Homo sapiens 100-103 2967288-9 1988 In the presence of Ca2+, the stoichiometry of the FP57-Trp.CaM complex was 1:1, FP57-Trp binding to CaM was competitive with neuromodulin. Tryptophan 85-88 calmodulin 1 Homo sapiens 59-62 2967288-9 1988 In the presence of Ca2+, the stoichiometry of the FP57-Trp.CaM complex was 1:1, FP57-Trp binding to CaM was competitive with neuromodulin. Tryptophan 85-88 calmodulin 1 Homo sapiens 100-103 3963824-4 1986 From measurements of the efficiencies of radiationless energy transfer from Trp-19 to the nitro derivatives of Tyr-99 and/or Tyr-138, it is concluded that Trp-19 is located in proximity to the C-terminal lobe of calmodulin in the complex. Tryptophan 155-158 calmodulin 1 Homo sapiens 212-222 2954960-11 1987 Both fragments have structural properties in common with the isolated calmodulin-binding domains of myosin light chain kinase: two cationic segments rich in hydrophobic residues, one constantly possessing a tryptophan, and the other exhibiting an amino acid sequence resembling sites phosphorylated by cAMP-dependent protein kinase. Tryptophan 207-217 calmodulin 1 Homo sapiens 70-80 4016082-3 1985 Changes in the fluorescence spectra, anisotropy, and accessibility of tryptophan whose indole side chain is on the apolar surface of the amphiphilic helix imply a significant role for the apolar surface in the binding of the mastoparans and another amphiphilic peptide, melittin, to calmodulin. Tryptophan 70-80 calmodulin 1 Homo sapiens 283-293 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 calmodulin 1 Homo sapiens 19-29 31124357-4 2019 We use Fourier transform infrared (FTIR) and ultrafast two-dimensional infrared (2D IR) spectroscopy of the carboxylate asymmetric stretching mode in calmodulin as a mutation- and label-independent probe of the conformational perturbations induced in calmodulin"s binding sites by two classes of mutation, tryptophan insertion and carboxylate side-chain deletion, commonly used to study ion binding in proteins. Tryptophan 306-316 calmodulin 1 Homo sapiens 150-160 32560560-2 2020 The aim of this study was to characterise interactions between the TRP cation channel subfamily melastatin member 4 (TRPM4) and endogenous intracellular modulators-calcium-binding proteins (calmodulin (CaM) and S100A1) and phosphatidylinositol 4, 5-bisphosphate (PIP2). Tryptophan 67-70 calmodulin 1 Homo sapiens 190-200 32560560-2 2020 The aim of this study was to characterise interactions between the TRP cation channel subfamily melastatin member 4 (TRPM4) and endogenous intracellular modulators-calcium-binding proteins (calmodulin (CaM) and S100A1) and phosphatidylinositol 4, 5-bisphosphate (PIP2). Tryptophan 67-70 calmodulin 1 Homo sapiens 202-205 28955897-4 2016 The affinity of the peptides for binding CaM followed the trend Baa (210+-10 pM)<(7-aza)Trp-Baa (109+-5 pM)<(2,7-aza)Trp-Baa (45+-2 pM), showing moderate increase in binding affinity upon increasing the number of nitrogen atoms in the Trp analogue. Tryptophan 91-94 calmodulin 1 Homo sapiens 41-44 29494137-4 2018 We show that in response to binding CaM, cSH2 exposes its tryptophan residue at the N-terminal region to the solvent. Tryptophan 58-68 calmodulin 1 Homo sapiens 36-39 28955897-5 2016 The increased binding affinity may be due to the formation of more hydrogen bonds upon binding CaM for the Trp analogue with more nitrogen atoms. Tryptophan 107-110 calmodulin 1 Homo sapiens 95-98 28955897-2 2016 In this study, we replaced the tryptophan in peptide Baa (LKWKKLLKLLKKLLKLG-NH2) with 7-azatryptophan or 2,7-diazatryptophan, forming (7-aza)Trp-Baa and (2,7-aza)Trp-Baa, to study the calmodulin (CaM)-peptide interaction. Tryptophan 31-41 calmodulin 1 Homo sapiens 184-194 28955897-2 2016 In this study, we replaced the tryptophan in peptide Baa (LKWKKLLKLLKKLLKLG-NH2) with 7-azatryptophan or 2,7-diazatryptophan, forming (7-aza)Trp-Baa and (2,7-aza)Trp-Baa, to study the calmodulin (CaM)-peptide interaction. Tryptophan 31-41 calmodulin 1 Homo sapiens 196-199 24495073-9 2014 Mutation of a conserved tryptophan (W831S) within the predicted CaM-binding site strongly reduced CaM binding. Tryptophan 24-34 calmodulin 1 Homo sapiens 64-67 27129269-8 2016 The residues of Trp-354, Arg-359, Glu-355, Leu-363, and Glu-367 in DR5 death domain that are important for DR5 recruitment of FADD and caspase-8 for DISC formation to signal apoptosis also play an important role for CaM-DR5 binding. Tryptophan 16-19 calmodulin 1 Homo sapiens 216-219 24495073-9 2014 Mutation of a conserved tryptophan (W831S) within the predicted CaM-binding site strongly reduced CaM binding. Tryptophan 24-34 calmodulin 1 Homo sapiens 98-101 18835080-6 2008 The Trp fluorescence intensities of mutated p21(141-164) peptides (F150W, Y151W and F159W) increased upon binding to Ca(2+)-saturated calmodulin and fluorescence maxima were blue shifted from 350 nm to 330 nm. Tryptophan 4-7 calmodulin 1 Homo sapiens 134-144 23755207-5 2013 Replacement of the tryptophan (W219) for alanine in i3, and phenylalanine (F309 or F313) for alanine in ct reduced their binding affinities for calmodulin, as predicted by computer docking simulations. Tryptophan 19-29 calmodulin 1 Homo sapiens 144-154 22767601-2 2012 CaM binds to either PMCA or C28 by a mechanism in which the primary anchor residue Trp-1093 binds to the C-terminal lobe of the extended CaM molecule, followed by collapse of CaM with the N-terminal lobe binding to the secondary anchor Phe-1110 (Juranic, N., Atanasova, E., Filoteo, A. G., Macura, S., Prendergast, F. G., Penniston, J. T., and Strehler, E. E. (2010) J. Biol. Tryptophan 83-86 calmodulin 1 Homo sapiens 0-3 22767601-2 2012 CaM binds to either PMCA or C28 by a mechanism in which the primary anchor residue Trp-1093 binds to the C-terminal lobe of the extended CaM molecule, followed by collapse of CaM with the N-terminal lobe binding to the secondary anchor Phe-1110 (Juranic, N., Atanasova, E., Filoteo, A. G., Macura, S., Prendergast, F. G., Penniston, J. T., and Strehler, E. E. (2010) J. Biol. Tryptophan 83-86 calmodulin 1 Homo sapiens 137-140 22767601-2 2012 CaM binds to either PMCA or C28 by a mechanism in which the primary anchor residue Trp-1093 binds to the C-terminal lobe of the extended CaM molecule, followed by collapse of CaM with the N-terminal lobe binding to the secondary anchor Phe-1110 (Juranic, N., Atanasova, E., Filoteo, A. G., Macura, S., Prendergast, F. G., Penniston, J. T., and Strehler, E. E. (2010) J. Biol. Tryptophan 83-86 calmodulin 1 Homo sapiens 137-140 22767601-6 2012 Using targeted molecular dynamics, we now show that dissociation of Ca(2+)-CaM from C28 may occur by a pathway in which Trp-1093, although deeply embedded in a pocket in the C-terminal lobe of CaM, leaves first. Tryptophan 120-123 calmodulin 1 Homo sapiens 75-78 19463840-1 2009 Melatonin is a modified tryptophan with potent biological activity, exerted by stimulation of specific plasma membrane (MT1/MT2) receptors, by lower affinity intracellular enzymatic targets (quinone reductase, calmodulin), or through its strong anti-oxidant ability. Tryptophan 24-34 calmodulin 1 Homo sapiens 210-220 18201104-3 2008 Complementary measurements take advantage of the unique conserved Trp within CaM-binding sequences that functions as a hydrophobic anchor in CaM binding and permits measurements of both a local and global peptide structure. Tryptophan 66-69 calmodulin 1 Homo sapiens 77-80 18201104-3 2008 Complementary measurements take advantage of the unique conserved Trp within CaM-binding sequences that functions as a hydrophobic anchor in CaM binding and permits measurements of both a local and global peptide structure. Tryptophan 66-69 calmodulin 1 Homo sapiens 141-144 17562702-5 2007 Tryptophan fluorescence spectroscopy showed that calcium-CaM binds to IQ motifs 1, 3, and 5 in a different conformation than apoCaM. Tryptophan 0-10 calmodulin 1 Homo sapiens 57-60 17905811-3 2007 Trp residue in melittin demonstrated drastic change in its dielectric relaxation rate and scale by binding with calmodulin. Tryptophan 0-3 calmodulin 1 Homo sapiens 112-122 11258955-1 2001 To follow Mg2+ binding to the N-terminal of calmodulin (CaM), we substituted Phe in position 19, which immediately precedes the first Ca2+/Mg2+ binding loop, with Trp, thus making F19WCaM (W-Z). Tryptophan 163-166 calmodulin 1 Homo sapiens 44-54 15697226-4 2005 Additionally, equilibrium titrations were used to measure the apparent dissociation constants of the various peptides with TA-calmodulin by changes in TA-calmodulin fluorescence and Trp fluorescence of the peptides. Tryptophan 182-185 calmodulin 1 Homo sapiens 126-136 11811958-8 2002 Studies with a synthetic peptide of this sequence demonstrated very tight Ca2+-dependent binding to CaM as judged by tryptophan fluorescence perturbation studies and phosphodiesterase activation by CaM. Tryptophan 117-127 calmodulin 1 Homo sapiens 100-103 11258955-1 2001 To follow Mg2+ binding to the N-terminal of calmodulin (CaM), we substituted Phe in position 19, which immediately precedes the first Ca2+/Mg2+ binding loop, with Trp, thus making F19WCaM (W-Z). Tryptophan 163-166 calmodulin 1 Homo sapiens 56-59 10792048-2 2000 To obtain structural information on this protein, we have engineered 10 tryptophan residues between positions 89 and 104 in the effector domain, a 24-residue-long amphipathic segment that mediates binding of MRP to CaM. Tryptophan 72-82 calmodulin 1 Homo sapiens 215-218 11054265-8 2000 Intrinsic tryptophan fluorimetry shows that two peptides, each of which includes one of the predicted regions, bind calmodulin: p17(11-25) binds calmodulin with a 2-to-1 stoichiometry and dissociation constant of approximately 10(-9) M(2), and p17(31-46) also binds calmodulin with a dissociation constant of about 10(-9) M. These binding sites are nearly contiguous, forming an extended calmodulin-binding domain p17(11-46). Tryptophan 10-20 calmodulin 1 Homo sapiens 116-126 11054265-8 2000 Intrinsic tryptophan fluorimetry shows that two peptides, each of which includes one of the predicted regions, bind calmodulin: p17(11-25) binds calmodulin with a 2-to-1 stoichiometry and dissociation constant of approximately 10(-9) M(2), and p17(31-46) also binds calmodulin with a dissociation constant of about 10(-9) M. These binding sites are nearly contiguous, forming an extended calmodulin-binding domain p17(11-46). Tryptophan 10-20 calmodulin 1 Homo sapiens 145-155 11054265-8 2000 Intrinsic tryptophan fluorimetry shows that two peptides, each of which includes one of the predicted regions, bind calmodulin: p17(11-25) binds calmodulin with a 2-to-1 stoichiometry and dissociation constant of approximately 10(-9) M(2), and p17(31-46) also binds calmodulin with a dissociation constant of about 10(-9) M. These binding sites are nearly contiguous, forming an extended calmodulin-binding domain p17(11-46). Tryptophan 10-20 calmodulin 1 Homo sapiens 145-155 11054265-8 2000 Intrinsic tryptophan fluorimetry shows that two peptides, each of which includes one of the predicted regions, bind calmodulin: p17(11-25) binds calmodulin with a 2-to-1 stoichiometry and dissociation constant of approximately 10(-9) M(2), and p17(31-46) also binds calmodulin with a dissociation constant of about 10(-9) M. These binding sites are nearly contiguous, forming an extended calmodulin-binding domain p17(11-46). Tryptophan 10-20 calmodulin 1 Homo sapiens 145-155 10072758-8 1999 Both CnB- and CaM-binding peptides have a high content of tryptophan and leucine, but CnB-binding peptides are more hydrophobic than CaM-binding peptides. Tryptophan 58-68 calmodulin 1 Homo sapiens 14-17 10072758-9 1999 CnB-binding peptides are negatively charged with clusters of hydrophobic residues rich in phenylalanine, whereas the CaM-binding peptides are positively charged and often contain an Arg/Lys-Trp motif. Tryptophan 190-193 calmodulin 1 Homo sapiens 117-120 10625668-6 2000 A point mutation in the C-terminal calmodulin-binding domain of gp160 (alanine 835 to tryptophan, A835W) eliminates gp160-dependent enhanced FAS-mediated apoptosis in transiently transfected cells, as well as in vitro calmodulin binding to a peptide corresponding to the C-terminal calmodulin-binding domain of gp160. Tryptophan 86-96 calmodulin 1 Homo sapiens 35-45 10679531-0 2000 Tryptophan fluorescence of calmodulin binding domain peptides interacting with calmodulin containing unnatural methionine analogues. Tryptophan 0-10 calmodulin 1 Homo sapiens 27-37 10679531-0 2000 Tryptophan fluorescence of calmodulin binding domain peptides interacting with calmodulin containing unnatural methionine analogues. Tryptophan 0-10 calmodulin 1 Homo sapiens 79-89 10679531-5 2000 Fluorescence quenching studies with added potassium iodide (KI) demonstrate that the non-native proteins limit the solvent accessibility of the Trp in the MLCK peptide to levels close to that of the wild-type CaM-MLCK interaction. Tryptophan 144-147 calmodulin 1 Homo sapiens 209-212 10679531-7 2000 In addition, we provide evidence that the nature of binding in the CaM-CaD B complex is unique compared with the other complexes studied, as the Trp residue of this peptide remains partially solvent exposed upon binding to CaM. Tryptophan 145-148 calmodulin 1 Homo sapiens 67-70 9931009-7 1999 The peptide binds with an alpha-helical structure to both lobes of Ca2+-saturated CaM, and the single Trp residue is firmly anchored into the C-terminal lobe of CaM. Tryptophan 102-105 calmodulin 1 Homo sapiens 161-164 9485473-6 1998 The Trp fluorescence quantum yield of many Trp-containing CaM-binding peptides increases upon binding to calcium-CaM. Tryptophan 4-7 calmodulin 1 Homo sapiens 58-61 9850564-5 1998 The effects of these ions on the substrate-binding ability of calmodulin have also been studied by fluorescence spectroscopy of the single tryptophan residue in a 22-residue synthetic peptide encompassing the skeletal muscle myosin light chain kinase calmodulin-binding domain. Tryptophan 139-149 calmodulin 1 Homo sapiens 62-72 9485473-0 1998 Tryptophan fluorescence quenching by methionine and selenomethionine residues of calmodulin: orientation of peptide and protein binding. Tryptophan 0-10 calmodulin 1 Homo sapiens 81-91 9485473-2 1998 In this work we have used fluorescence spectroscopy to study the role of these Met residues in binding the single Trp residue that is found in many CaM-binding domain peptides. Tryptophan 114-117 calmodulin 1 Homo sapiens 148-151 9485473-6 1998 The Trp fluorescence quantum yield of many Trp-containing CaM-binding peptides increases upon binding to calcium-CaM. Tryptophan 4-7 calmodulin 1 Homo sapiens 113-116 9485473-6 1998 The Trp fluorescence quantum yield of many Trp-containing CaM-binding peptides increases upon binding to calcium-CaM. Tryptophan 43-46 calmodulin 1 Homo sapiens 58-61 9485473-6 1998 The Trp fluorescence quantum yield of many Trp-containing CaM-binding peptides increases upon binding to calcium-CaM. Tryptophan 43-46 calmodulin 1 Homo sapiens 113-116 9485473-9 1998 The fluorescence results obtained with these four CaM variants showed that Se is very effective at quenching Trp fluorescence in the calmodulin-bound peptides from myosin light chain kinase (MLCK) and CaM kinase I, while S is somewhat effective (Se > S > C). Tryptophan 109-112 calmodulin 1 Homo sapiens 50-53 9485473-9 1998 The fluorescence results obtained with these four CaM variants showed that Se is very effective at quenching Trp fluorescence in the calmodulin-bound peptides from myosin light chain kinase (MLCK) and CaM kinase I, while S is somewhat effective (Se > S > C). Tryptophan 109-112 calmodulin 1 Homo sapiens 133-143 9485473-9 1998 The fluorescence results obtained with these four CaM variants showed that Se is very effective at quenching Trp fluorescence in the calmodulin-bound peptides from myosin light chain kinase (MLCK) and CaM kinase I, while S is somewhat effective (Se > S > C). Tryptophan 109-112 calmodulin 1 Homo sapiens 201-204 9485473-11 1998 Since the Trp fluorescence quenching is very dramatic, the protein containing Leu"s in the C-terminal domain and SeMet"s in the N-terminal domain allowed us to directly determine the orientation of the MLCK and CaM kinase I peptides bound to CaM; in both cases the Trp residue binds to the C-terminal domain of CaM. Tryptophan 265-268 calmodulin 1 Homo sapiens 211-214 9038155-2 1997 Since shortening the side chains of Trp-800, Arg-812, and Leu-813 in smooth muscle myosin light chain kinase abrogated calmodulin-dependent activation (Bagchi, I. C., Huang, Q., and Means, A. R. (1992) J. Biol. Tryptophan 36-39 calmodulin 1 Homo sapiens 119-129 9214312-2 1997 Tryptophan was introduced in position 92 of the calmodulin mutants as a fluorescent label to monitor the calcium-induced structural changes in the C-terminal domain of calmodulin. Tryptophan 0-10 calmodulin 1 Homo sapiens 48-58 9214312-2 1997 Tryptophan was introduced in position 92 of the calmodulin mutants as a fluorescent label to monitor the calcium-induced structural changes in the C-terminal domain of calmodulin. Tryptophan 0-10 calmodulin 1 Homo sapiens 168-178 9395448-5 1997 The point mutant M124Q located in the C-terminal domain of CaM produced a 57-fold increase in the CaM activation constant for CaMKI and suggests the involvement of methionine 124 in an important hydrophobic interaction with tryptophan 303 of CaMKI. Tryptophan 224-234 calmodulin 1 Homo sapiens 59-62 9395448-5 1997 The point mutant M124Q located in the C-terminal domain of CaM produced a 57-fold increase in the CaM activation constant for CaMKI and suggests the involvement of methionine 124 in an important hydrophobic interaction with tryptophan 303 of CaMKI. Tryptophan 224-234 calmodulin 1 Homo sapiens 98-101 8687382-8 1996 Ca2+ -calmodulin produced a broadening in the signals of the NMR spectrum of the 10 kDa Ca(2+)-calmodulin-binding C-terminal fragment of caldesmon arising from tryptophans -749 and -779 and caused an enhancement of maximum tryptophan fluorescence of 49% and a 16 nm blue shift of the maximum. Tryptophan 160-171 calmodulin 1 Homo sapiens 6-16 9003189-0 1997 Tryptophan residues in caldesmon are major determinants for calmodulin binding. Tryptophan 0-10 calmodulin 1 Homo sapiens 60-70 9003189-1 1997 Calmodulin has been shown to interact with the COOH-terminal domain of gizzard h-caldesmon at three sites, A (residues 658-666), B (residues 687-695), and B" (residues 717-725), each of which contains a Trp residue [Zhan et al. Tryptophan 203-206 calmodulin 1 Homo sapiens 0-10 9003189-13 1997 Replacing Trp 659 at site A or Trp 692 at site B to Ala reduces binding by 22- and 31-fold (Kd = 2.9 x 10(-6) and 4.0 x 10(-6) M), respectively, and destabilizes the CaD39-calmodulin complex by 1.75 and 1.94 kcal mol-1, respectively. Tryptophan 10-13 calmodulin 1 Homo sapiens 172-182 9003189-13 1997 Replacing Trp 659 at site A or Trp 692 at site B to Ala reduces binding by 22- and 31-fold (Kd = 2.9 x 10(-6) and 4.0 x 10(-6) M), respectively, and destabilizes the CaD39-calmodulin complex by 1.75 and 1.94 kcal mol-1, respectively. Tryptophan 31-34 calmodulin 1 Homo sapiens 172-182 9003189-19 1997 Taken together, these results suggest that Trp 659 and Trp 692 are the major determinants in the caldesmon-calmodulin interaction and that Trp 722 in site B" plays a minor role. Tryptophan 43-46 calmodulin 1 Homo sapiens 107-117 9003189-19 1997 Taken together, these results suggest that Trp 659 and Trp 692 are the major determinants in the caldesmon-calmodulin interaction and that Trp 722 in site B" plays a minor role. Tryptophan 55-58 calmodulin 1 Homo sapiens 107-117 9003189-19 1997 Taken together, these results suggest that Trp 659 and Trp 692 are the major determinants in the caldesmon-calmodulin interaction and that Trp 722 in site B" plays a minor role. Tryptophan 55-58 calmodulin 1 Homo sapiens 107-117 8898856-0 1996 Heme-CO binding to tryptophan-containing calmodulin mutants. Tryptophan 19-29 calmodulin 1 Homo sapiens 41-51 8898856-1 1996 The binding of heme-CO to genetically engineered calmodulin containing a single tryptophan residue has been studied. Tryptophan 80-90 calmodulin 1 Homo sapiens 49-59 8687382-8 1996 Ca2+ -calmodulin produced a broadening in the signals of the NMR spectrum of the 10 kDa Ca(2+)-calmodulin-binding C-terminal fragment of caldesmon arising from tryptophans -749 and -779 and caused an enhancement of maximum tryptophan fluorescence of 49% and a 16 nm blue shift of the maximum. Tryptophan 160-171 calmodulin 1 Homo sapiens 95-105 8687382-8 1996 Ca2+ -calmodulin produced a broadening in the signals of the NMR spectrum of the 10 kDa Ca(2+)-calmodulin-binding C-terminal fragment of caldesmon arising from tryptophans -749 and -779 and caused an enhancement of maximum tryptophan fluorescence of 49% and a 16 nm blue shift of the maximum. Tryptophan 160-170 calmodulin 1 Homo sapiens 6-16 8687382-8 1996 Ca2+ -calmodulin produced a broadening in the signals of the NMR spectrum of the 10 kDa Ca(2+)-calmodulin-binding C-terminal fragment of caldesmon arising from tryptophans -749 and -779 and caused an enhancement of maximum tryptophan fluorescence of 49% and a 16 nm blue shift of the maximum. Tryptophan 160-170 calmodulin 1 Homo sapiens 95-105 8635738-6 1996 268 (1993) 23025-23030] using a library displaying random peptides 15 aa in length identified CaM-binding peptides which contained a Trp-Pro dipeptide motif. Tryptophan 133-136 calmodulin 1 Homo sapiens 94-97 8563635-6 1995 Comparison of 1H-NMR spectra of CaM bound to WFF, a Trp 4-->Phe analogue (FFF), or a Trp 4-->Phe/Phe 17-->Trp analogue (FFW) suggests that all three peptides bind to CaM in the same orientation, i.e., with the peptide side chain in position 4 interacting with the C-domain and the side chain in position 17 interacting with the N-domain. Tryptophan 52-55 calmodulin 1 Homo sapiens 32-35 8563635-8 1995 Molecular modeling/energy minimization studies indicate that only minor local changes in the protein structure are required to accommodate binding of the bulkier Trp 17 side chain of the FFW peptide to the N-domain of CaM. Tryptophan 162-165 calmodulin 1 Homo sapiens 218-221 8562872-9 1995 It seems likely that the toxin binds to tryptophan in the calmodulin-binding domain, thus causing a reduction in the rate at which this domain can interact with Ca(2+)-calmodulin or acidic phospholipids. Tryptophan 40-50 calmodulin 1 Homo sapiens 58-68 8562872-9 1995 It seems likely that the toxin binds to tryptophan in the calmodulin-binding domain, thus causing a reduction in the rate at which this domain can interact with Ca(2+)-calmodulin or acidic phospholipids. Tryptophan 40-50 calmodulin 1 Homo sapiens 168-178 8071370-4 1994 Interactions between CaM and variant Phe-37-->Trp can be monitored by fluorescence spectroscopy, allowing us to determine, by competitive assays, the relative affinities of the wild-type and variant proteins for calmodulin. Tryptophan 49-52 calmodulin 1 Homo sapiens 21-24 8071370-4 1994 Interactions between CaM and variant Phe-37-->Trp can be monitored by fluorescence spectroscopy, allowing us to determine, by competitive assays, the relative affinities of the wild-type and variant proteins for calmodulin. Tryptophan 49-52 calmodulin 1 Homo sapiens 215-225