ライフサイエンスコーパス: myoglobin

1 s (Human Serum Albumin, creatine kinase, and myoglobin).

2 vity in a heme-nonheme biosynthetic model in myoglobin.

3 ed and thus providing a more detailed map of myoglobin.

4 er proteins, exemplified by cytochrome c and myoglobin.

5 ficant differences relative to the wild type myoglobin.

6 mit of 2.7 on the iron(IV)hydroxide pK(a) in myoglobin.

7 acetonitrile and acid unfolding pathways of myoglobin.

8 cating surpassing performance as compared to myoglobin.

9 ne serum albumin, cytochrome C, lysozyme and myoglobin.

10 e three-dimensional structure of sperm whale myoglobin.

11 the two-state folding proteins, Rnase A and myoglobin.

12 e all significantly impaired in mice without myoglobin.

13 r structures including metallo-proteins like myoglobin.

14 ved from a common ancestor to hemoglobin and myoglobin.

15 ectrum of CO bound to the heme of His-tagged myoglobin.

16 u) and three histidines (His) in sperm whale myoglobin.

17 was found for zinc/iron transmetallation in myoglobin.

18 with the secondary and tertiary structure of myoglobin.

19 ctive site of NOR, into the distal pocket of myoglobin.

20 f a neutral thiol-heme model complex but not myoglobin.

21 arged model peptides and a tryptic digest of myoglobin.

22 referentially nitrates Tyr103 in horse heart myoglobin.

23 e dynamical pathways for ligand migration in myoglobin.

24 er carbon monoxide (CO) photodissociation in myoglobin.

25 34 patients had elevated creatine kinase or myoglobin.

26 ell with a blue shift from 410 to 408 nm for myoglobin.

27 ing transport and storage by hemoglobins and myoglobins.

28 common ancestor of mammalian hemoglobins and myoglobins.

29 nce of fragmentation of ubiquitin (8.6 kDa), myoglobin (17 kDa), and carbonic anhydrase (29 kDa) upon

30 The labeling of myoglobin (17 kDa), transferrin (77 kDa), and thyroglobu

31 The triplet state of the myoglobin ((3)MMb) created by intersystem crossing from

32 f NO. from nitrite reduction by deoxygenated myoglobin activates canonical soluble guanylate cyclase/

33 appreciable rate in the presence of reduced myoglobin alone.

34 r fluorescently labeled proteins, ubiquitin, myoglobin, alpha-1-acid glycoprotein and lysozyme, were

35 s two partially disordered states, i.e., apo-myoglobin (aMb) at pH 7 and pH 4.

36 was loss of abundance relative to uncrowded myoglobin analyzed using conventional HX-MS, 97% coverag

37 The two proteins investigated are myoglobin and beta-lactoglobulin, which are prototypical

38 aneous quantification of cardiac biomarkers (myoglobin and cardiac troponin I) in the clinically sign

39 SI measurement revealed charge reduction for myoglobin and cytochrome c as a function of increasing p

40 Moreover, the chemosensor selectivity to the myoglobin and cytochrome c interferences was excellent w

41 ion reveals that the ion signal detected for myoglobin and cytochrome c reaches a plateau and then be

42 A muFFE separation of myoglobin and cytochrome c was also demonstrated on a 3D

43 Myoglobin and cytochrome c were well resolved and gave r

44 ng muFFE separations of Chromeo P503 labeled myoglobin and cytochrome c.

45 Exquisitely engineered myoglobin and cytochrome P450 enzymes can generate these

46 Hypoxic vasodilation studies in myoglobin and endothelial and inducible NO synthase knoc

47 logy is applied to study cavity structure in myoglobin and five of its mutants.

48 fferent distal pocket mutants of sperm whale myoglobin and found to be governed by the ease of rotati

49 e conducted directed evolution of the Ir(Me)-myoglobin and generated mutants that form either enantio

50 These changes, in conjunction with lower myoglobin and glycogen contents, Myh4 and GAPDH transcri

51 ess (W-MR-Al) contained the lowest remaining myoglobin and haem iron content and also showed the lowe

52 at shows only minor sequence similarity with myoglobin and hemoglobin but conforms to the typical 3-o

53 Respiratory proteins such as myoglobin and hemoglobin can, under oxidative conditions

54 e 54 years since the first excitement of the myoglobin and hemoglobin structures in 1960.

55 an that of the 5-coordinate hemes present in myoglobin and hemoglobin.

56 ifferences at the iron edge for solutions of myoglobin and hemoglobin.

57 NT-Pt/Mb) for the direct electrochemistry of myoglobin and its application towards determination of h

58 Generally, lower myoglobin and lipid contents were found in protein isola

59 by the analysis of noncovalently bound holo-myoglobin and of ribonuclease B.

60 Thus, the sarcoplasmic fraction contained myoglobin and several enzymes that are essential for eff

61 nsport proteins (fatty acid-binding protein, myoglobin and somatic cytochrome-C) and others (creatine

62 uction of nitrite to nitric oxide by cardiac myoglobin and subsequent S-nitrosation of mitochondrial

63 In parallel tests, cardiac myoglobin and troponin I, the AMI biomarkers, were deter

64 lpha-helical globin fold, similar to that of myoglobin and Vgb from Vitreoscilla stercoraria.

65 for melittin, 100% for cytochrome c, 90% for myoglobin, and 65% for bovine serum albumin.

66 ply charged ions of cytochrome c, ubiquitin, myoglobin, and bovine serum albumin formed by electrospr

67 four model proteins: melittin, cytochrome c, myoglobin, and bovine serum albumin.

68 eraction of carbon monoxide with hemoglobin, myoglobin, and components of the respiratory chain.

69 ined for three different proteins (Trp-cage, myoglobin, and cytochrome c) with folding time constants

70 ce of the passage of carbon monoxide through myoglobin, and explains the nonexponential time dependen

71 Good-quality ESI-MS spectra of cytochrome c, myoglobin, and lysozyme as test proteins in a saline sol

72 Controlled alignment of streptavidin (STV), myoglobin, and nanoparticles with nanometer resolution h

73 m analogous to that observed for hemoglobin, myoglobin, and neuroglobin.

74 The monoclonal anti-myoglobin antibody (ab-Mb) was covalently immobilized us

75 Control tests using non-specific myoglobin antigen confirmed the specificity of the prese

76 Using myoglobin as a model protein, we show that this method c

77 In this paper we propose myoglobin as a powerful molecular marker to evaluate the

78 e short time scale (picoseconds) dynamics of myoglobin as a result of His tag incorporation.

79 Here we demonstrate, using myoglobin as an example, a general route to grow a PEG-l

80 proving the suitability of using immobilized myoglobin as electrocatalyst in the nitrite reduction pr

81 ities, we have tracked structural changes in myoglobin as it undergoes a photolysis-induced transitio

82 The obtained results show that using myoglobin as marker, 5% (25 mg/500 mg) of pork or beef m

83 By using myoglobin as marker, low amounts (0.50mg/0.50g, w/w; app

84 current work addresses this question, using myoglobin as model system.

85 The myoglobin autoxidation rate increased with increasing st

86 Using rational design, an engineered myoglobin-based catalyst capable of catalyzing the cyclo

87 methodology enables the rapid development of myoglobin-based cyclopropanation biocatalysts featuring

88 Here, we use a set of myoglobin-based functional HCO models to investigate the

89 e using an assay that combines catalase with myoglobin binding kinetics.

90 n systems including: ribonuclease (Rnase) A, myoglobin, bovine carbonic anhydrase (BCA) II, hemoglobi

91 ontaining four model proteins (cytochrome c, myoglobin, bovine serum albumin (BSA), and beta-casein)

92 ontaining bradykinin, leucine enkephalin and myoglobin, but loss of the heme group from myoglobin occ

93 monitor the mild denaturation of horse heart myoglobin by acetonitrile, and the results showed good a

94 determined in the presence of reduced deoxy-myoglobin by measuring the formation of carboxy-myoglobi

95 ing enzymes, was engineered into sperm whale myoglobin by replacing Leu29 and Phe43 with Glu and His,

96 urements of proteins (BSA, apomyoglobin, and myoglobin) by these HPsensors display much stronger sign

97 Using a functional oxidase model in myoglobin called F33Y-Cu(B)Mb that contains an engineere

98 have shown that globins like hemoglobin and myoglobin can also oxidize H2S to thiosulfate and hydrop

99 Up to 20% of myoglobin can be nitrosylated under gastro-intestinal co

100 d gaseous CF3CHN2 is processed by engineered myoglobin catalysts expressed in bacterial cells.

101 Engineered variants of sperm whale myoglobin catalyze this synthetically valuable C-C bond-

102 methyl-substituted cyclopropanes by means of myoglobin-catalyzed olefin cyclopropanation reactions in

103 afast structural changes in the carbonmonoxy myoglobin complex upon photolysis of the Fe-CO bond.

104 The computed electronic structure of the myoglobin complexes and the nature of the Fe-O2 bonding

105 proteins, we have probed the active site of myoglobin compound II over the pH range of 3.9-9.5, usin

106 volutionary underpinnings of the high muscle myoglobin concentration phenotype of divers.

107 that is mechanistically linked with maximal myoglobin concentration.

108 This work shows that myoglobin constitutes a promising and robust scaffold fo

109 me E degrees in a functional model of CcO in myoglobin containing three histidines and one tyrosine i

110 In particular, we prepared modified myoglobins containing an Ir(Me) site that catalyse the f

111 O synthase knockout models suggest that only myoglobin contributes to systemic hypoxic vasodilatory r

112 lobin fold similar to that of hemoglobin and myoglobin could act as O2 sensors.

113 en between this intermediate and horse heart myoglobin Cpd II.

114 were used to increase sample throughput; 930 myoglobin crystals mounted at random orientation inside

115 Using myoglobin, cytochrome c, and beta-2-microglobulin as mod

116 comparison of the mass spectral response for myoglobin, cytochrome c, and lysozyme is presented for l

117 The soret band of myoglobin decreased with a concomitant decrease in the r

118 and ribonuclease A) and six acidic proteins (myoglobin, deoxyribonuclease I, beta-lactoglobulin A, be

119 luated using seven doubly-labeled mutants of myoglobin designed to monitor selected interhelical dist

120 used marked changes in the peak currents for myoglobin detection.

121 tial using 38 singly spin-labeled mutants of myoglobin distributed throughout the sequence.

122 d-coordination states of the heme complex in myoglobin during the preconditioning of ex vivo cardiomy

123 Its reduction to NO. via the heme globin myoglobin enhances blood flow and matches O(2) supply to

124 In this study, we report that myoglobin exhibits a similar capacity for sulfide oxidat

125 Sperm whale myoglobin forms a hydroperoxide on Tyr-151 in a hydrogen

126 port of multiply charged ions of the protein myoglobin, frequently used as a standard in TW IM-MS stu

127 The approach is introduced by use of myoglobin from four meats: beef, pork, horse and lamb.

128 The binding of NO to myoglobin, giving a 6-coordinate ferrous-heme complex, w

129 (i) cyclostome hemoglobin + cytoglobin, (ii) myoglobin + globin E, (iii) globin Y, and (iv) the alpha

130 Myoglobin has an important physiological role in vertebr

131 within the heme distal pocket of sperm whale myoglobin has offered well-defined diiron clusters for t

132 Aplysia fasciata myoglobin, having no naturally occurring tyrosines but 1

133 For protein complexes myoglobin.heme (17.6 kDa) and dihydrofolate reductase.me

134 ight into the nature of the binding sites of myoglobin/heme, eIF4E/m(7)GTP, and human peptidyl-prolyl

135 eading to increased voltammetric signals for myoglobin, hemoglobin, and cytochrome c.

136 Reaction rate constants for myoglobin, hemoglobin, neuroglobin, and flavohemoglobin

137 ormers were compared to those of native holo-myoglobin (hMb) at pH 7 and extensively unfolded aMb at

138 ecularly imprinted polymer film (MIP), viz., myoglobin-imprinted electropolymerized poly(o-phenylened

139 The myoglobin in both quail species contained eight histidin

140 rmal levels of type I fiber markers MyH7 and myoglobin in Fnip1-null mice.

141 equire a CO acceptor, believed to be reduced myoglobin in Mb-CO assays, in order to facilitate the re

142 en developed to detect the presence of horse myoglobin in raw meat samples.

143 We have shown that deoxygenated myoglobin in the heart can reduce nitrite to nitric oxid

144 reases the lipid peroxidase activity of this myoglobin in the presence of low concentrations of reduc

145 might be due to the concentration of H2S by myoglobin in this tissue.

146 estigate the conformation and flexibility of myoglobin in three folded and partially folded states.

147 Simulations were conducted on myoglobin in water, water/sulfolane, and water/m-NBA.

148 -step redox reaction of the surface-confined myoglobin, in a deaerated 0.1 M phosphate buffer, pH 7.

149 ages that markedly grow from cytochrome c to myoglobin indicate the dipole alignment of rare conforme

150 , as well as the loss of the heme group from myoglobin, indicate that a fraction of the protein popul

151 und in the iron-histidine stretching mode of myoglobin, indicating that the proximal ligand of iNOS(P

152 the micron outer diameter tips, but some apo-myoglobin ions are produced with the submicron tips.

153 A single charge-state distribution of holo-myoglobin ions is produced by nanoESI from a slightly ac

154 the Fe-O(2) center in oxy-hemoglobin and oxy-myoglobin is a long-standing issue in the field of bioin

155 The hemoprotein myoglobin is a model system for the study of protein dyn

156 On the basis of recent observations that myoglobin is expressed in the vasculature of hypoxia-tol

157 We show in the present study that myoglobin is expressed in vascular smooth muscle and con

158 trospray ionization (nESI) conditions, where myoglobin is sprayed from an aqueous solution buffered t

159 oximal site, equivalent to the Xe1 cavity in myoglobin, is never visited.

160 k is focused on the two more expressed human myoglobin isoforms.

161 When compared with chicken myoglobin, Japanese quail showed 98% sequence identity,

162 he N-terminus of the robust globular protein myoglobin leads to only minor changes to the electrostat

163 properties of room-temperature solvent-free myoglobin liquids with near-native structure and reversi

164 realization of room-temperature solvent-free myoglobin liquids with retained function presents novel

165 The proteins myoglobin, lysozyme, and albumin were used to evaluate t

166 del mixture of proteins including ovalbumin, myoglobin, lysozyme, and cytochrome c as well as a monoc

167 iply charged intact nitrated protein ions of myoglobin, lysozyme, and cytochrome c in a commercial Fo

168 Standard proteins myoglobin (m/z-value 16,950) and ribonuclease B (m/z-val

169 Immobilized myoglobin maintained a high affinity for nitric oxide (K

170 Surprisingly, O2 binding to myoglobin (Mb) also induces elevated HDX rates.

171 ace formed by physiological partner proteins myoglobin (Mb) and cytochrome b(5) (b(5)) reveal interpr

172 use in modulating complex formation between myoglobin (Mb) and cytochrome b(5) (b(5)).

173 200 ppm) in washed mince (pH 6), with added myoglobin (Mb) and haemoglobin (Hb), from bighead carp (

174 bited (carboxy), and O2-bound (oxy) hemes in myoglobin (MB) and hemoglobin (HB) solutions and in porp

175 of CO binding in other heme systems such as myoglobin (Mb) and hemoglobin (Hb).

176 w involving a metal-substituted (M = Mg, Zn) myoglobin (Mb) and its physiological partner protein, cy

177 larly imprinted polymer (MIP) templated with myoglobin (Mb) and the reference non-imprinted polymer (

178 ngle crystal of the nitrite adduct of ferric myoglobin (Mb) at 100 K to high-intensity synchrotron X-

179 so able to use human serum albumin (HSA) and myoglobin (Mb) but not hemopexin as iron sources.

180 fer (ET) within a "charge-disproportionated" myoglobin (Mb) dimer with greatly enhanced affinity.

181 Myoglobin (Mb) double mutant T67R/S92D displays peroxida

182 trocatalytic kinetics of covalently attached myoglobin (MB) films on magnetic nanoparticles (MB-MNP(c

183 For example, the ferrous heme protein myoglobin (Mb) has been shown to reduce nitrite (NO(2)(-

184 At onset of muscle contraction, myoglobin (Mb) immediately releases its bound O2 to the

185 Electroanalysis of myoglobin (Mb) in 10 plasma samples of healthy donors (H

186 dicated that long-chain fatty acids can bind myoglobin (Mb) in an oxygen-dependent manner.

187 Monitoring of myoglobin (Mb) in human blood serum is highly in demand

188 uctuations that occur in hemoglobin (Hb) and myoglobin (Mb) in solution.

189 Sperm whale myoglobin (Mb) in the ferric state has a peroxidase acti

190 , we showed that the muscle-specific protein myoglobin (Mb) interacts with complex IV.

191 Myoglobin (Mb) is a model system for ligand binding and

192 ctrochemical detection of cardiac bio-marker myoglobin (Mb) on aptamer functionalized rGO/CNT nanostr

193 The removal of the heme group from myoglobin (Mb) results in a destabilization of the prote

194 l, and butyl isocyanide bound to sperm whale myoglobin (Mb) reveal two major conformations.

195 Since the elucidation of the myoglobin (Mb) structure, a histidine residue on the E h

196 We prepared a myoglobin (Mb) triple mutant (D44K/D60K/E85K; Mb(+6)) su

197 transfer (ET) from a suite of Zn-substituted myoglobin (Mb) variants to cytochrome b(5) (b(5)).

198 of the midpoint potential of skeletal horse myoglobin (Mb) with a heme-bound fluoride ion (Mb-F) rev

199 the proteins alpha-Lactalbumin (alphaLA) and myoglobin (Mb) with the biosurfactant rhamnolipid (RL).

200 rode (GCE) for the quantitative detection of myoglobin (Mb), a cardiac marker for acute myocardial in

201 y a particular fold originally identified in myoglobin (Mb), characterize the "hemoglobin (Hb) superf

202 s, e.g. urease, glucose oxidase, hemoglobin, myoglobin (Mb), conjugation with metals e.g. gold (Au),

203 own that muscle specific O2 binding protein, Myoglobin (Mb), is localized in mitochondria and interac

204 bovine serum albumin (BSA), heme-containing myoglobin (Mb), monoclonal antibody against viral protei

205 ing protein structure or redox properties of myoglobin (Mb).

206 tely 2125 cm(-1) upon binding to sperm whale myoglobin (Mb).

207 Mb, a functional model of HCOs engineered in myoglobin (Mb).

208 analogous fashion, CN(-), CO, and O2 bind to myoglobin (Mb).

209 globin by measuring the formation of carboxy-myoglobin (Mb-CO).

210 It was recently demonstrated that in ferric myoglobins (Mb) the fluorescence quenching of the photoe

211 ary widely for naturally occurring mammalian myoglobins (Mb).

212 de H/D exchange in a representative protein (myoglobin, Mb).

213 Moreover, the scope of this myoglobin-mediated transformation could be extended to t

214 s(4-sulfonatophenyl)porphyrinate) and ferric myoglobin (metMb) to quantitatively yield [Mn(TPPS)(NO)]

215 ascertain whether these two almost identical myoglobins might exert different functions and to contri

216 e hydrogen-bond effect on HNO in MbHNO (Mb = myoglobin) models.

217 Myoglobin motions within the hybrid are found to closely

218 hing between two well defined substates of a myoglobin mutant is observed on the approximately 50-ps

219 an be detected within the distal cavities of myoglobin mutants by subtle changes in the absorbance sp

220 phosphazine (m/z 1422) and a 19-fold charged myoglobin (MW 16.9 kDa), respectively.

221 e way, consisting by the immobilization of a myoglobin (My) - single walled carbon nanotubes (SWCNT)

222 tandard proteins (e.g. cytochrome C (Cyt-C), myoglobin (MYO) and bovine serum albumin (BSA)) have bee

223 ollowing a bottom-up approach, for targeting myoglobin (Myo) in a point-of-care context.

224 onin T (TnT), bovine serum albumin (BSA) and myoglobin (Myo) in the performance of the sensor was tes

225 igh-sensitivity troponin T, creatine kinase, myoglobin, N-terminal B-type natriuretic peptide, C-reac

226 nimum model for CcO, a mutant of sperm whale myoglobin, named Cu(B)Mb, has been engineered, in which

227 an adaptive molecular signature of elevated myoglobin net surface charge in diving species that is m

228 tions, and on the other a different yield of myoglobin-NO formation was experimentally observed throu

229 The iron/zinc exchange in myoglobin occurring during maturation of Parma hams seem

230 d myoglobin, but loss of the heme group from myoglobin occurs as a result of the denaturing solution

231 ime scale and also alters protein motions of myoglobin on the slower, >100 ps time scale, as demonstr

232 Hemoproteins, hemoglobin and myoglobin, once released from cells can cause severe oxi

233 pendent amber nonsense codons in sperm whale myoglobin or green fluorescent protein.

234 of DHP is high relative to that of wild-type myoglobin or hemoglobin, but the most definitive differe

235 noconjugates consisting of globular cores of myoglobin or lysozyme and demonstrate that the derived s

236 Here, we tested the hypothesis that myoglobin overexpressing transgenic mice (MbTg(+)) exhib

237 differences between groups, indicating that myoglobin overexpression does not affect arteriogenesis.

238 combined effect of pH (from 7.2 to 3.2) and myoglobin oxidation state was evaluated in the reaction

239 The interrelationship between myoglobin oxidation, lipid oxidation and discolouration

240 Overall, lipid and myoglobin oxidations in oxeye scad occurred in a concurr

241 smic protein content, especially extractable myoglobin (p<0.05).

242 by measuring the HX-MS signal intensities of myoglobin peptides from crowded samples containing 300 g

243 Similarly, films of myoglobin physisorbed on magnetic nanoparticles (MB/MNP(

244 Notably, the myoglobin-poly(OEGMA) conjugate [hydrodynamic radius (R(

245 sociated with the heme prosthetic group in a myoglobin-polymer surfactant solvent-free liquid are inv

246 cells (hMSCs) with synthetic membrane-active myoglobin-polymer-surfactant complexes can provide a res

247 hways of diffusion of a CO molecule inside a myoglobin protein and toward the solvent are investigate

248 of ligand binding and discrimination in the myoglobin protein.

249 tandem mass spectrometry (MS/MS) on a large myoglobin proteolytic peptide (8 kDa) provides a resolut

250 In addition, fluoride binding in myoglobin provides a stabilization of -1.9 kcal/mol of t

251 An ultrafast increase of myoglobin radius of gyration occurs within 1 picosecond

252 han reported for Vitreoscilla hemoglobin and myoglobin, respectively.

253 oxyferrous hemoglobin A (HbA) and oxyferrous myoglobin, respectively.

254 with bovine serum albumin or equine skeletal myoglobin resulted in vesicles with similar asymmetric m

255 The single mutation differentiating the two myoglobins resulted in strongly affecting the plasticity

256 lled carbon nanotubes-platinum nanoparticles/myoglobin (RGO-MWCNT-Pt/Mb) for the direct electrochemis

257 ther small nonpolar ligands move between the myoglobin's buried heme, which is the ligand binding sit

258 First, the methodology was tested on myoglobin's CO migration, and the results were compared

259 o contribute to a deeper understanding about myoglobin's oxygen-level dependent functioning, they hav

260 sing conventional HX-MS, 97% coverage of the myoglobin sequence was still obtained.

261 Its application to a membrane protein and to myoglobin show that the approach is sensitive to protein

262 The immobilized myoglobin-silk protein film was stable and could be stor

263 of type I fibers characterized by increased myoglobin, slow twitch markers [myosin heavy chain 7 (My

264 Sequence analysis revealed both species' myoglobin structures consist of 153 amino acids, differi

265 d resting levels of ATP, phosphocreatine and myoglobin, suggesting that sildenafil improves dystrophi

266 domyolysis) is accompanied by the release of myoglobin that becomes deposited in the kidney, causing

267 Here, we use a biosynthetic model of HCO in myoglobin that selectively binds different non-haem meta

268 termining the three-dimensional structure of myoglobin, the first solved structure of a protein, fund

269 In myoglobin, this reaction is thought to proceed through a

270 evidence of such 'proteinquake' observed in myoglobin through femtosecond X-ray solution scattering

271 ective variable space for CO localization in myoglobin to estimate the kinetics of entry, exit, and i

272 xic vasodilation via reactions with vascular myoglobin to form NO..

273 facilitated by limited pepsin proteolysis of myoglobin to open a reaction channel for metal exchange

274 coefficients, 0.9901, 0.9921, and 0.9980 for myoglobin, transferrin, and thyroglobulin, respectively,

275 rom three procedure blanks were obtained for myoglobin, transferrin, and thyroglobulin, respectively.

276 In vitro, myoglobin treatment induced proximal tubular cells to se

277 roteins and mixtures of up to five proteins (myoglobin, troponin C, actin, bovine serum albumin (BSA)

278 B-33, however, was very similar to a genuine myoglobin-type molecule.

279 The extent of unfolding of holo-myoglobin upon rapid mixing with theta-glass emitters is

280 vity, resulting in the identification of the myoglobin variant Mb(L29S,H64V,V68F), which is capable o

281 Reported herein is that engineered myoglobin variants can catalyze the olefination of aldeh

282 tegy was implemented and applied to engineer myoglobin variants capable of providing access to 1-carb

283 ms of these products could be obtained using myoglobin variants featuring stereodivergent selectivity

284 ctra are reported for Fe(III)(NO) adducts of myoglobin variants with altered polarity in the distal h

285 Myoglobin was embedded in transparent honeybee silk prot

286 effect of immobilization on the structure of myoglobin was fully investigated using UV/visible, Fouri

287 Japanese quail myoglobin was isolated from quail cardiac muscles, purif

288 approximately 10(-9)M) for the detection of myoglobin was obtained.

289 Ferrous myoglobin was oxidized by sulfur trioxide anion radical

290 age of molecular biology had just begun, and myoglobin was the only protein with a known high-resolut

291 The separation of both horse and beef myoglobins was achieved in only seven minutes.

292 sv) for hemin, cytochrome c, hemoglobin, and myoglobin were 5.6x10(7), 1.7x10(7), 1.6x10(7), and 6.2x

293 nces of Japanese quail and northern bobwhite myoglobin were deduced by cDNA cloning of the coding seq

294 t analogous to correction of heme binding by myoglobin when its proximal histidine is mutated.

295 We use site-directed mutants of myoglobin, where both the distal Cu and the redox-active

296 Mixing acid-denatured myoglobin with an aqueous ammonium acetate solution to i

297 also used to replace a native salt bridge in myoglobin with an intramolecular crosslink to a proximal

298 the remote site or nitrite bioactivation by myoglobin within the target organ abrogated the cardiopr

299 ensional structure of a protein, sperm-whale myoglobin, worthy of a Nobel Prize in Chemistry in 1962.

300 that redox cycling between ferric and ferryl myoglobin yields radical species that cause severe oxida