ライフサイエンスコーパス: myoglobin

1 aminotransferase 1, C-reactive protein, and myoglobin).

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

3 er carbon monoxide (CO) photodissociation in myoglobin.

4 34 patients had elevated creatine kinase or myoglobin.

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

6 charge ladders" of azurin, cytochrome c, and myoglobin.

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

8 er proteins, exemplified by cytochrome c and myoglobin.

9 ficant differences relative to the wild type myoglobin.

10 mple two-protein mixture of cytochrome c and myoglobin.

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

12 acetonitrile and acid unfolding pathways of myoglobin.

13 cating surpassing performance as compared to myoglobin.

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

15 e three-dimensional structure of sperm whale myoglobin.

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

17 e all significantly impaired in mice without myoglobin.

18 er reduction potential compared to wild-type myoglobin.

19 nI or cTnT), creatine kinase-MB (CK-MB), and myoglobin.

20 DI-TOF-MS that ZnPP formation takes place in myoglobin.

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

22 r structures including metallo-proteins like myoglobin.

23 was found for zinc/iron transmetallation in myoglobin.

24 common ancestor of mammalian hemoglobins and myoglobins.

25 h the respiratory function in hemoglobin and myoglobins.

26 benzofuran cyclopropanation with engineered myoglobins.

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

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

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

30 ncreased levels at the start of MP (medians: myoglobin: 4377 ng/mL, CK: 1442 U/L), peaking 6 h after

31 aking 6 h after perfusate exchange (medians: myoglobin: 9206 ng/mL, CK: 3995 U/L) at timepoint 24.

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

33 r smaller proteins (ubiquitin, cytochrome c, myoglobin) again resemble those at AP, producing feature

34 appreciable rate in the presence of reduced myoglobin alone.

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

36 ESI of acid-unfolded apo-myoglobin (aMb) in the presence of sulfolane produced ch

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

38 emperature aqueous solution containing 10 uM myoglobin and 5 ug mL(-1) trypsin is electrosonically sp

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

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

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

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

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

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

45 Myoglobin and cytochrome c were well resolved and gave r

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

47 Exquisitely engineered myoglobin and cytochrome P450 enzymes can generate these

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

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

50 We also simulated transport times for myoglobin and found that they were remarkably similar be

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

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

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

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

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

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

57 The systems investigated were myoglobin and its noncovalently bound heme cofactor, and

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

65 Tested on cytochrome c, myoglobin, and beta-lactoglobulin cross-linked using BS(

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 interleukin-2 receptor, indirect bilirubin, myoglobin, and fibrinogen degradation products.

71 or two clinically relevant proteins, p53 and myoglobin, and for pathogenic and benign missense varian

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

73 While hemin, wild-type myoglobin, and other hemoproteins are unable to catalyze

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 well established that low concentrations of myoglobin are aberrantly expressed in a significant prop

77 Hemoglobin and myoglobin are oxygen-binding proteins with S = 0 heme {F

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

79 , these results elucidate a new function for myoglobin as a modulator of mitochondrial dynamics and r

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

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

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

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

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

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

86 and thionine acetate as redox mediators and myoglobin as the analyte, we demonstrate that normal pul

87 The myoglobin autoxidation rate increased with increasing st

88 ination with whole-cell transformations, the myoglobin-based biocatalyst was used for the asymmetric

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

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

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

92 Myoglobin binds O(2,) facilitates its intracellular tran

93 We report the development of engineered myoglobin biocatalysts for executing asymmetric intramol

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

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

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

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

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

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

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

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

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

103 um acetate (pH 6.9), several proteins (i.e., myoglobin, carbonic anhydrase, and cytochrome c) could b

104 s, and one patient had associated widespread myoglobin casts.

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

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

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

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

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

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

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

112 that is mechanistically linked with maximal myoglobin concentration.

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

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

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

116 tochrome c oxidase activities, and increased myoglobin content.

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

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

119 Myoglobin, creatine-kinase (CK) showed increased levels

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

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

122 when bound to the heme proteins hemoglobin, myoglobin, cytochrome P450 and cytochrome c, respectivel

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

124 dynamics and reveal a novel pathway by which myoglobin decreases breast cancer cell proliferation and

125 pin (HS, S = 2) pentacoordinated domed deoxy-myoglobin (deoxyMb) form upon ligand detachment from the

126 y, increased mitofusin expression was due to myoglobin-dependent free-radical production, leading to

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

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

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

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

131 Myoglobin, encoded by MB, is a small cytoplasmic globula

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

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

134 ated this pathway in a murine model in which myoglobin-expressing xenografts exhibited decreased tumo

135 on high resolution structural information of myoglobin, for the unfolded and even for the molten glob

136 n the dark with addition of FeCl(2)/H(2)O(2)/myoglobin (forced oxidation).

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

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

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

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

141 cal characterization reveals that the mutant myoglobin has altered O(2) binding, exhibits a faster he

142 Myoglobin has an important physiological role in vertebr

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

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

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

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

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

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

149 for the efficient hydrolysis of horse heart myoglobin (HHM) in low buffer concentrations.

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

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

152 The myoglobin in both quail species contained eight histidin

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

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

155 emonstrate in vitro that expression of human myoglobin in MDA-MB-231, MDA-MB-468, and MCF7 breast can

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

157 pectra of the Fe(II)/Fe(III) redox couple of myoglobin in reduction and oxidation NPSV modes were in

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

159 The myoglobin in the meat did not influence the assays perfo

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

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

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

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

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

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

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

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

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

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

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

171 Myoglobin is a monomeric heme protein expressed ubiquito

172 xpressed only at low levels in these tumors, myoglobin is associated with attenuated tumor growth and

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

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

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

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

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

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

179 negative breast tumor tissues, mitofusin and myoglobin levels were positively correlated.

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

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

182 Myoglobin maturation is driven by the hsp90 chaperone ma

183 Preliminary studies show that mutant myoglobin may result in elevated superoxide levels at th

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

185 200 ppm) in washed mince (pH 6), with added myoglobin (Mb) and haemoglobin (Hb), from bighead carp (

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

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

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

189 Peptides originating from myoglobin (Mb) and myosin (My) were analyzed using multi

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

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

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

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

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

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

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

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

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

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

200 Myoglobin (Mb) maturation involves heme incorporation as

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

219 t cancer patients, but the mechanism of this myoglobin-mediated protection against further cancer gro

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

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

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

223 Myoglobin motions within the hybrid are found to closely

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

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

226 ific and specific proteins including cardiac myoglobin (MYG), bovine serum albumin (BSA) and cardiac

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

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

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

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

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

232 Here we probe them in the case of Myoglobin-NO (MbNO) using element- and spin-sensitive fe

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

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

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

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

237 e diffusion rates of lysozyme, cytochrome c, myoglobin, ovalbumin, bovine serum albumin, and etanerce

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

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

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

241 The interrelationship between myoglobin oxidation, lipid oxidation and discolouration

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

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

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

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

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

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

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 rein, we report a signaling pathway by which myoglobin regulates mitochondrial dynamics and thereby d

253 han reported for Vitreoscilla hemoglobin and myoglobin, respectively.

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

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

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

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

258 ns are unable to catalyze this reaction, the myoglobin scaffold could be remodeled by protein enginee

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

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

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

262 overage for three standard proteins, namely, myoglobin, SiLuLite mAb, and NIST mAb.

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 iological catalysts derived from sperm whale myoglobin that exploit a carbene transfer mechanism for

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

268 Focusing on myoglobin, the current work solves this problem by disse

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

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 the reaction of azide with microcrystalline myoglobin, using only a fraction of the sample required

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

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

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

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

285 of the active site via protein engineering, myoglobin variants with stereodivergent selectivity were

286 Myoglobin was embedded in transparent honeybee silk prot

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

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

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

290 Ferrous myoglobin was oxidized by sulfur trioxide anion radical

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

292 Myoglobin was used as the main model protein, and eluent

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

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

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

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

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

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

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

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