ライフサイエンスコーパス: sperm whale

1 thesis for this low diversity, especially in sperm whales.

2 For example, sperm whales, a species that remains for long periods at

3 salt dependence of histidine pK(a) values in sperm whale and horse myoglobin and in histidine-contain

4 eight species of delphinids, pygmy and dwarf sperm whales, and harbor porpoises, but not in beluga or

5 s and of canyons and seamounts to beaked and sperm whales, and quantified seasonal shifts in the dens

6 an all-alpha-helical single domain protein, Sperm whale apomyoglobin (apoMb).

7 propensity of the completely helical protein sperm whale apomyoglobin (sw ApoMb) for amyloid formatio

8 rapidly than its eukaryotic analogues (e.g., sperm whale apomyoglobin and soybean apoleghemoglobin),

9 s, and kinetics of heat-induced unfolding of sperm whale apomyoglobin core formation have been studie

10 The overall affinity of sperm whale apomyoglobin for hemin is approximately 1 x

11 ormation on isotopically labeled recombinant sperm whale apomyoglobin in the native state at pH 6.1.

12 The F helix region of sperm whale apomyoglobin is disordered, undergoing confo

13 ues corresponding to the C-terminal helix of sperm whale apomyoglobin.

14 stabilities approaching that of recombinant sperm whale apomyoglobin.

15 ies of the folding and unfolding kinetics of sperm whale apomyoglobin.

16 in the acid-induced unfolding of recombinant sperm whale apomyoglobin.

17 The social relationships of sperm whales are organized in a multilevel society with

18 obins from diving mammals, particularly from sperm whales, are the most stable, whereas the apoprotei

19 -rebinding behavior of single crystal native sperm whale carbonmonoxy myoglobin (swMbCO) (space group

20 Infrared spectra of heme-bound CO in sperm whale carbonmonoxy myoglobin and two mutants (H64L

21 erties of the three taxonomic A substates of sperm whale carbonmonoxy myoglobin in 75% glycerol/buffe

22 around the alpha-gamma axis of the heme, of sperm-whale carbonmonoxy myoglobin in water.

23 ated vibrational echo data were obtained for sperm whale carbonmonoxymyoglobin (MbCO) at 300 K.

24 the effects of heme rotational isomerism in sperm-whale carbonmonoxymyoglobin using computational te

25 To determine if it does, we selected sperm whale cementum to provide large anisotropic substr

26 methods, and large-scale redistributions of sperm whale cultural clans in the Pacific have likely ch

27 NepsilonH is found to be similar to that in sperm whale cyanomet myoglobin.

28 fts for the heme methyls of low-spin, ferric sperm whale cyanometmyoglobin reconstituted with a varie

29 Slices of sperm whale dentin were mechanically polished and surfac

30 cket mutations at the E7 position (His64) of sperm whale deoxymyoglobin (deoxyMb) are used as a probe

31 f 10 different distal heme pocket mutants of sperm whale deoxymyoglobin (deoxyMb) has been investigat

32 the zinc-containing diamagnetic analogue of sperm whale deoxymyoglobin has been measured as a functi

33 terception of predator vocalizations by male sperm whales disrupted functional behaviours and mediate

34 X) in single cysteine-containing variants of sperm whale ferric aquomyoglobin.

35 Sixteen sperm whales from calves to large adults showed a size-r

36 data are reported for the cavity mutants of sperm whale H93G myoglobin and human H25A heme oxygenase

37 ance excreted by the intestinal tract of the sperm whale, has been a highly prized fragrance ingredie

38 ransmission seems key in the partitioning of sperm whales into sympatric clans.

39 ups at the 2- and 4-positions of the heme in sperm whale Mb and HRP, and examine the structural and b

40 Introduction of a nonaxial His into sperm whale Mb at the topologically equivalent position

41 HNE became covalently bound to sperm whale Mb at up to five sites based on ESI-MS analy

42 the oxidation and binding rate constants for sperm whale Mb were increased when His(E7) was replaced

43 In contrast to sperm whale Mb, where the orientation of the magnetic ax

44 perature, although more plastic than that of sperm whale Mb.

45 GuHCl-induced, equilibrium unfolding of five sperm whale metMb variants, which were selected to exami

46 A series of proximal side mutants of sperm whale metmyoglobin (metMb) that involves residues

47 Reaction of sperm whale metmyoglobin (SwMb) with H2O2 produces a fer

48 In the sperm whale metmyoglobin Tyr103Phe mutant, there is no d

49 hydrogen peroxide with human methemoglobin, sperm whale metmyoglobin, and horse heart metmyoglobin w

50 udies on an engineered heme-copper center in sperm whale myoglobin (Leu-29 --> HisPhe-43 --> His, cal

51 Sperm whale myoglobin (Mb) in the ferric state has a per

52 ethyl, propyl, and butyl isocyanide bound to sperm whale myoglobin (Mb) reveal two major conformation

53 N HMQC spectra were collected on 15N-labeled sperm whale myoglobin (Mb) to determine the tautomeric s

54 nd approximately 2125 cm(-1) upon binding to sperm whale myoglobin (Mb).

55 , 106-116/E(d), and of a dominant epitope of sperm whale myoglobin (SWM), 102-118/A(d), is entirely d

56 ndent reaction of lactoperoxidase (LPO) with sperm whale myoglobin (SwMb) or horse myoglobin (HoMb) p

57 > Phe and Trp --> Phe mutants of recombinant sperm whale myoglobin (SwMb) were investigated.

58 ected mice in response to a non-parasite Ag, sperm whale myoglobin (SwMb).

59 cell populations demonstrated that a diverse sperm whale myoglobin 110-121-reactive CD4(+) T cell rep

60 Hybridoma 74a.e9 was specific for the sperm whale myoglobin 67-79 peptide and could be partial

61 Equivalent mutations in sperm whale myoglobin alter ligand affinity by only 5-fo

62 ies of 20 different distal pocket mutants of sperm whale myoglobin and found to be governed by the ea

63 this work, molecular dynamics simulations of sperm whale myoglobin and mutations at positions 68 (E11

64 eractions in the distal pockets of wild-type sperm whale myoglobin and soybean leghemoglobin.

65 protein G, for the lambda repressor and for sperm whale myoglobin are presented.

66 pectra were measured in the visible bands of sperm whale myoglobin as a function of distal pocket mut

67 iron-containing enzymes, was engineered into sperm whale myoglobin by replacing Leu29 and Phe43 with

68 Engineered variants of sperm whale myoglobin catalyze this synthetically valuab

69 o soybean Lba, whereas the same mutations in sperm whale myoglobin cause 50 to 100-fold decreases in

70 ce, previously observed in the isoelectronic sperm whale myoglobin complex.

71 d pH 7, soybean Lba is much less stable than sperm whale myoglobin due both to a fourfold higher rate

72 On the whole, the results for the sperm whale myoglobin E7 substitutions show that the rat

73 Sperm whale myoglobin forms a hydroperoxide on Tyr-151 i

74 ciated carbon monoxide in the heme pocket of sperm whale myoglobin has been studied using equilibrium

75 Fe(B) site within the heme distal pocket of sperm whale myoglobin has offered well-defined diiron cl

76 A circular permutein of sperm whale myoglobin in which the G helix is C-terminal

77 engineered heme-copper center in myoglobin (sperm whale myoglobin L29H/F43H, called Cu(B)Mb).

78 on tryptophan through the use of recombinant sperm whale myoglobin labeled with 13C at the indole rin

79 can be exchanged into the proximal cavity of sperm whale myoglobin mutant H93G, providing a simple me

80 In the sperm whale myoglobin mutant H93G, the proximal histidin

81 o three independent amber nonsense codons in sperm whale myoglobin or green fluorescent protein.

82 water molecule in the distal heme pocket of sperm whale myoglobin over the pH range 4.3-9.4.

83 the deoxy, oxy, and aquomet forms of native sperm whale myoglobin reconstituted with cobalt protopor

84 Engineering these three residues into sperm whale myoglobin results in a triple mutant with ap

85 bin, we determined the crystal structures of sperm whale myoglobin to 2.0 A or better in different st

86 ion of carbon monoxide in the heme pocket of sperm whale myoglobin was studied by using molecular dyn

87 asts with H-D amide exchange measurements on sperm whale myoglobin which indicated low protection for

88 seen when asparagine68 is inserted into H64L sperm whale myoglobin which lacks a distal histidine.

89 The computations are performed both in sperm whale myoglobin wild-type and in sperm whale V68F

90 ansfer via a tyrosine residue (tyrosine 103, sperm whale myoglobin).

91 L heme domain, elephant myoglobin, wild-type sperm whale myoglobin, and sperm whale myoglobins having

92 (B6 X A)F1 mice were immunized with sperm whale myoglobin, and T cell clones and hybridomas

93 electrochemical midpoints (E(m)s) at pH 7 in sperm whale myoglobin, Aplysia myoblogin, hemoglobin I,

94 histidines not interacting with the heme in sperm whale myoglobin, it was found that seven (His-12,

95 As a minimum model for CcO, a mutant of sperm whale myoglobin, named Cu(B)Mb, has been engineere

96 To measure these interactions in sperm whale myoglobin, single mutations were made to dis

97 ggests that the radical resides on Tyr151 in sperm whale myoglobin, Tyr133 in soybean leghemoglobin,

98 In a simulation of sperm whale myoglobin, we found 294 such high-density re

99 secretion of gamma-interferon (IFN-gamma) by sperm whale myoglobin-specific Th1 cells of DBA/2 mouse

100 onstants, respectively, compared to those of sperm whale myoglobin.

101 of wild-type Lba were compared with those of sperm whale myoglobin.

102 exit onto the three-dimensional structure of sperm whale myoglobin.

103 utamates (Glu) and three histidines (His) in sperm whale myoglobin.

104 wild-type DHP and has comparable activity to sperm whale myoglobin.

105 dynamics of the heme pocket of a recombinant sperm whale myoglobin.

106 ees C, approximately 35 times faster than in sperm whale myoglobin.

107 pathways for ligand movement into and out of sperm whale myoglobin.

108 - and off-rates are also similar to those of sperm whale myoglobin.

109 scaris hemoglobin is very similar to that in sperm whale myoglobin.

110 r to that of leghemoglobin a than to that of sperm whale myoglobin.

111 n the oxygen dissociation rate compared with sperm whale myoglobin.

112 t of the CO derivative of several mutants of sperm whale myoglobin.

113 ve the 3-dimensional structure of a protein, sperm-whale myoglobin, worthy of a Nobel Prize in Chemis

114 dation of a variety of different recombinant sperm whale myoglobins (Mb) and human hemoglobins (Hb).

115 globin, wild-type sperm whale myoglobin, and sperm whale myoglobins having alanine, valine, threonine

116 The properties of wild-type, V68T, and H97D sperm whale myoglobins were compared to determine the re

117 ement of coordinated water from H64 and H64Q sperm whale myoglobins, where the E7 side chain hydrogen

118 Distal pocket mutants of sperm whale oxymyoglobin (oxy-Mb) were reacted with a 2.

119 or behaviour of five typically-solitary male sperm whales (Physeter macrocephalus) in the Norwegian S

120 es to dive away from the perceived predator, sperm whales responded to killer whale playbacks by inte

121 th in sperm whale myoglobin wild-type and in sperm whale V68F myoglobin mutant, which is experimental

122 pygmy (Kogia breviceps) and dwarf (K. sima) sperm whales were used to characterize the gut microbiom