24 research outputs found
A Systemic Functional Study of the Head Identification of the English Nominal Group
Head identification is the first and crucial step in describing and analyzing the English nominal group. The literature to date indicates that the way of identifying the Head of the English nominal group varies from one school of linguistics to another and even from one grammarian to another. This paper focuses on the English nominal group containing the word of and the research is conducted from the systemic functional linguistics perspective
Chiral metallo-supramolecular complexes selectively recognize human telomeric G-quadruplex DNA
Here, we report the first example that one enantiomer of a supramolecular cylinder can selectively stabilize human telomeric G-quadruplex DNA. The P-enantiomer of this cylinder has a strong preference for G-quadruplex over duplex DNA and, in the presence of sodium, can convert G-quadruplexes from an antiparallel to a hybrid structure. The compound's chiral selectivity and its ability to discriminate quadruplex DNA have been studied by DNA melting, circular dichroism, gel electrophoresis, fluorescence spectroscopy and S1 nuclease cleavage. The chiral supramolecular complex has both small molecular chemical features and the large size of a zinc-finger-like DNA-binding motif. The complex is also convenient to synthesize and separate enantiomers. These results provide new insights into the development of chiral anticancer agents for targeting G-quadruplex DNA
μ€κ΅μΈ νκ΅μ΄ νμ΅μλ₯Ό μν μΈλμ΄ κ΅μ‘ μ°κ΅¬-μ‘°μ΄λ² νμ©μ μ€μ¬μΌλ‘-
νμλ
Όλ¬Έ (μμ¬)-- μμΈλνκ΅ λνμ : κ΅μ΄κ΅μ‘κ³Ό, 2017. 2. ꡬ본κ΄.μΈκ΅μ΄λ‘ μμ¬μν΅μ νκΈ° μν΄μ λ°μμ΄λ λ¬Έλ²μ λν νμ΅λΏλ§ μλλΌ μ΄νμ λν νμ΅μ΄ μ€μνλ€. μ΄νλ μ΄μ’
μ λ°λΌ νμμ΄, κ³ μ μ΄, μΈλμ΄μ μΈ κ°μ§ μ’
λ₯λ‘ κ΅¬λΆλλ€. νκ΅ μ¬νμ κΈκ²©ν κ΅μ νλ μΈμ΄ μ¬μ©μλ ν° μν₯μ λ―ΈμΉκ³ μλλ° νΉν μΈλμ΄κ° μΌμμμ μ°¨μ§νλ λΉμ¨μ λμμ§κ³ μμΌλ©°, μ΄μ λ°λΌ νκ΅μ΄ νμ΅μκ° μΈλμ΄λ₯Ό μ ν κΈ°νλ λ§μμ§κ³ μλ€. μ΄ μ°κ΅¬λ μ€κ΅μΈ νκ΅μ΄ νμ΅μλ€μ μΈλμ΄μ λν μ΄ν΄ λ₯λ ₯ λ° μ¬μ© λ₯λ ₯μ ν₯μνκ³ μ μΈλμ΄ κ΅μ‘μ νμμ±μ νΌλ ₯νκ³ , μ‘°μ΄λ² νμ©μ μ€μ¬μΌλ‘ νλ μΈλμ΄ κ΅μ‘μ λ΄μ©κ³Ό λ°©μμ λͺ¨μνλ λ°μ κ·Έ λͺ©μ μ΄ μλ€.
νκ΅μ΄μμλ μΈλμ΄ μμ μμ μ κ·Έλλ‘ νκΈ°νμ¬ μμμ κ°κΉμ΄ λͺ¨μ΅μ μ μ§νκ³ μλ€. λ°λ©΄μ, μ€κ΅μ΄μμλ κ°μΈκ° λ€μ΄μλ μ£Όμ μμ λ§ νκΈ°ν¨μΌλ‘μ¨ μμ μ λν μΆμνλ νΉμ§μ 보μ΄κ³ μλ€. μ΄λ¬ν μ°¨μ΄μ μΌλ‘ μΈνμ¬ μ€κ΅μΈ νμ΅μκ° νκ΅μ΄ μΈλμ΄λ₯Ό μ΄ν΄νλ λ° μ΄λ €μμ΄ μλ€. κ·Έλ¦¬κ³ ννμ μΈ μΈ‘λ©΄μμ νκ΅μ΄ μΈλμ΄λ νμ, ν©μ±, νμ¬μ μ€λ³΅, μλ΅, μ μ‘°μ΄ λ± λ€μν ꡬ쑰 μ νμ΄ μκΈ° λλ¬Έμ νμ΅μκ° μ΄ν΄νκΈ°μ μ΄λ €μμ΄ λ°λ₯Έλ€. νΉν, λ¨μΌ μΈλμ΄λ³΄λ€ μΈλμ΄μ λ€λ₯Έ μ΄μ’
μ λ¨μ΄λ μ μ¬λ₯Ό κ²°ν©νμ¬ κ΅¬μ±λ ν©μ±μ΄, νμμ΄μ κ΅¬μ‘°κ° λ 볡μ‘νκΈ° λλ¬Έμ νκ΅μ΄ μ‘°μ΄λ²μ λν μΈμμ΄ λΆμ‘±νλ©΄ μΈλμ΄ μλ―Έλ₯Ό μ΄ν΄νκΈ° μ΄λ €μΈ κ²μ΄λ€. μ΄μ κ°μ λ¬Έμ μμμμ μΆλ°νμ¬ μ΄ μ°κ΅¬μμλ μ€κ΅μΈ νμ΅μμ μΈλμ΄ μ΄ν΄ λ₯λ ₯μ ν₯μνκΈ° μν΄ ν¨κ³Όμ μΈ μΈλμ΄ κ΅μ‘ λ΄μ©κ³Ό λ°©μμ ꡬμνκ³ μ νμλ€.
β
‘μ₯μμλ μ ν μ°κ΅¬λ₯Ό ν λλ‘ λ¨Όμ νκ΅μ΄ μΈλμ΄μ κ°λ
κ³Ό μ νμ λν΄ μ΄ν΄λ³΄μλ€. κΈ°μ‘΄ μ°κ΅¬μ μ μμ λΆλ₯ κΈ°μ€μ μ 리νμ¬ νκ΅μ΄ μΈλμ΄μ μ μλ₯Ό λ΄λ¦¬κ³ μ‘°μ΄λ²μ λ°λΌ μΈλμ΄λ₯Ό μ νλ³λ‘ λΆλ₯νμλ€. κ·Έλ¦¬κ³ ννμ μΈ‘λ©΄μμ νκ΅μ΄ μΈλμ΄μ μ€κ΅μ΄ μΈλμ΄λ₯Ό λμ‘° λΆμνμλ€. λν μ€κ΅μμ μ΄λ£¨μ΄μ§κ³ μλ νκ΅μ΄ μΈλμ΄μ κ΅μ‘ νν©μ λΆμνμλ€. κ΅μ‘ νν© λΆμμ μν΄ μ€κ΅μμ μΆνλ νκ΅μ΄ κ΅μ¬λ₯Ό μ΄ν΄λ³΄κ³ νμ΅μ μ€λ¬Έμ μ€μνμλ€. ꡬ체μ μΌλ‘λ μ€κ΅ λ΄ λνμμ μ¬μ©νκ³ μλ κ΅μ¬λ₯Ό λΆμνμ¬ κ΅μ¬μμ νκ΅μ΄ μΈλμ΄λ₯Ό μ΄λ»κ² μ μνκ³ μλμ§λ₯Ό κΈ°μ νμλ€. λν μ€κ΅ λνμ μ¬ν μ€μΈ μ€κ΅μΈ νμ΅μμκ² κ΅μ νμ΅ μ€ν μ‘°μ¬λ₯Ό μ€μν¨μΌλ‘μ¨ νκ΅μ΄ μΈλμ΄ νμ΅μ λν νλ λ° νμ΅μμ μ΄λ €μ λ±μ μ‘°μ¬νμλ€. μ€λ¬Έ μ‘°μ¬λ₯Ό ν λλ‘ μ€κ΅μΈ νμ΅μμ νκ΅μ΄ μΈλμ΄μ λν μ΄ν΄ λ° μΈμ, νμ΅ κ²½λ‘, μμ
μμμ νμ΅ λ°©μ λ±μ λνμ¬ λΆμνκ³ κ·Έ λ΄μ©μ μ μνμλ€. μ΄μ΄μ νκ΅μ΄ μΈλμ΄ μ¬μ λ° μ΄ν μλ£λ₯Ό λ°νμΌλ‘ νκ΅μ΄ κ΅μ‘μ© μΈλμ΄ λͺ©λ‘μ μ μ νκ³ λμ΄λλ₯Ό μ μνμλ€.
β
’μ₯μμλ μ€λ¬Έ μ‘°μ¬μ μΈν°λ·°λ₯Ό ν΅νμ¬ μ€κ΅μΈ μ€κΈ νμ΅μμ νκ΅μ΄ μΈλμ΄ μ΄ν΄ μμμ μ μνμλ€. μ΄λ₯Ό μνμ¬ λ¨Όμ β
‘μ₯μμ λ
Όμν μ΄λ‘ μ λ°νμΌλ‘ μ€λ¬Έμ§λ₯Ό μμ±νμ¬ νμ΅μμ μΈλμ΄ μ΄ν μμ λ₯λ ₯, μ§μ λ₯λ ₯, κ·Έλ¦¬κ³ μ 체 μ΄ν΄ λ₯λ ₯μ μ΄ν΄λ³Έ ν, μ€λ₯μ μμΈμ ꡬ체μ μΌλ‘ νμ
νκΈ° μν΄ μ¬ν μΈν°λ·°λ₯Ό μννμλ€. κ·Έλ¦¬κ³ μμ§λ μλ£μ κ²°κ³Όλ₯Ό λΆμνκΈ° μν΄ ν΅κ³ νλ‘κ·Έλ¨μ μ¬μ©νμλ€.
β
£μ₯μμλ β
’μ₯μμ μ΄ν΄λ³Έ κ²°κ³Όλ₯Ό λ°μνμ¬ νκ΅μ΄ μΈλμ΄ κ΅μ‘μ λͺ©μ λ° λͺ©νλ₯Ό μ μνμκ³ ν¨κ³Όμ μΈ μΈλμ΄ κ΅μΒ·νμ΅ λ΄μ©μ ꡬμΆνμλ€. μ΄λ₯Ό μν΄, μ‘°μ΄λ²(μ΄κ·Ό, μ μ¬ λ± λ¨μ) λ° μΈλμ΄ μ‘°μ΄ μ νμ λν μ΄ν΄ κ΅μ‘, μ‘°μ΄λ² μ§μμ νμ©ν μΈλμ΄μ νν νΉμ§μ λΆμ κ΅μ‘, μΌλΆ μΈλμ΄ νκΈ°λ²μ λν κ°μ‘° κ΅μ‘, μΈλμ΄ μλ―Έμ μμ΄ μμ΄ λ° μ€κ΅μ΄ μΈλμ΄ μλ―Έμ λΉκ΅ μ€λͺ
κ΅μ‘, κ·Έλ¦¬κ³ μλ―Έλ§ κ΅¬μΆ λ° μ΄κ·Όμ΄λ μ μ¬ νμ©μ ν΅ν μλ‘μ΄ λ¨μ΄μ μμ± κ΅μ‘ λ΄μ©μ ꡬμνμλ€. λν μ€μ κ΅μ‘ νμ₯μμ μ μ©ν μ μλλ‘ νꡬ νλμ μ€μνλ 'OHE(κ΄μ°°-κ°μ€-μ€ν)' λͺ¨νμ μ¬μ©νμ¬ μ‘°μ΄λ² νμ©μ μ€μ¬μΌλ‘ νλ μΈλμ΄ κ΅μΒ·νμ΅ λͺ¨νκ³Ό κ΅μ€ νλμ λ§λ ¨νκ³ κ·Έ κ΅μ‘μ ν¨κ³Όλ₯Ό κ²μ¦νμλ€.
λ³Έ μ°κ΅¬λ μ€κ΅μΈ νμ΅μμ μΈλμ΄ μ‘°μ΄ μ νμ λΆμνμλ€λ μ κ³Ό μ‘°μ΄λ²μ νμ©νμ¬ μΈλμ΄λ₯Ό μμ±νκ±°λ μλ―Έλ₯Ό μ μΆνμλ€λ μ μμ μμκ° μλ€. μμΈλ¬ μ€κ΅μΈ νμ΅μλ€μ΄ μΈλμ΄λ₯Ό μ‘°μ΄ μ νμ λ°λΌ λΆλ₯νκ³ μ½κ² κΈ°μ΅ν λΏ μλλΌ μ₯κΈ°μ μΌλ‘ κΈ°μ΅ν μ μκΈ° μνμ¬ ν¨κ³Όμ μΈ μΈλμ΄ κ΅μΒ·νμ΅ λ°©λ²μ λͺ¨μνλ€λ μ μμλ μμκ° μλ€.β
. μλ‘ 1
1. μ°κ΅¬μ νμμ± λ° λͺ©μ 1
2. μ ν μ°κ΅¬ 4
2.1. μΈλμ΄μ λν κ΅μ΄νμ μ°κ΅¬ 4
2.2. μΈλμ΄μ λν νκ΅μ΄ κ΅μ‘νμ μ°κ΅¬ 6
3. μ°κ΅¬ λμ λ° μ°κ΅¬ λ°©λ² 7
β
‘. μΈλμ΄ κ΅μ‘ μ°κ΅¬λ₯Ό μν μ μ 11
1. μΈλμ΄μ κ°λ
κ³Ό μ ν 11
1.1. μΈλμ΄μ κ°λ
12
1.2. μ‘°μ΄λ²μ λ°λ₯Έ μΈλμ΄μ μ ν 20
2. νκ΅μ΄μ μ€κ΅μ΄ μΈλμ΄μ ννμ λμ‘° λΆμ 50
2.1. μμ΄ ννμ νκ΅μ΄μ μ€κ΅μ΄ μΈλμ΄ 52
2.2. μ½μ΄ ννμ νκ΅μ΄μ μ€κ΅μ΄ μΈλμ΄ 57
2.3. ν©μ± ννμ νκ΅μ΄μ μ€κ΅μ΄ μΈλμ΄ 59
2.4. νμ ννμ νκ΅μ΄μ μ€κ΅μ΄ μΈλμ΄ 62
3. μ€κ΅ λ΄ νκ΅μ΄ μΈλμ΄ κ΅μ‘ νν© 66
3.1. μ€κ΅μμ μΆνλ νκ΅μ΄ κ΅μ¬ λΆμ 66
3.2. μΈλμ΄ μμ
μ λν νμ΅μμ μΈμ 76
4. νκ΅μ΄ κ΅μ‘μ© μΈλμ΄ λͺ©λ‘μ μ μ 79
4.1. νκ΅μ΄ κ΅μ‘μ© μΈλμ΄ λͺ©λ‘ μ μ μ νν© 79
4.2. νκ΅μ΄ κ΅μ‘μ© μΈλμ΄ λͺ©λ‘ μ μ λ° λμ΄λ μ€μ 80
β
’. νμ΅μμ μΈλμ΄ μ΄ν΄ μμ λ° μ€λ₯ λΆμ 88
1. μ‘°μ¬ λ°©λ² λ° μ μ°¨ 88
1.1. μ‘°μ¬ μ°Έμ¬μ μ 보 88
1.2. μ‘°μ¬ λ°©λ² λ° μλ£ κ΅¬μ± 90
2. μ‘°μ¬ κ²°κ³Ό λ° λΆμ 94
2.1. μΈλμ΄ μ‘°μ΄λ²μ λν μ‘°μ¬ κ²°κ³Ό λΆμ 94
2.2. μΈλμ΄ μ΄ν μμ λ₯λ ₯μ μ‘°μ¬ κ²°κ³Ό λΆμ 97
2.3. μΈλμ΄ μ΄ν λ₯λ ₯(μμ &μ§μ λ₯λ ₯)μ μ‘°μ¬ κ²°κ³Ό λΆμ 101
3. νμ΅μμ μ€λ₯ μμΈ λΆμ 113
3.1. λͺ¨κ΅μ΄μ λͺ©νμ΄μ λ¨μ΄ ꡬ쑰 μ°¨μ΄λ₯Ό μΈμνμ§ λͺ»ν μ€λ₯ 113
3.2. μΈμ΄μ μμΈκ³Ό λΉμΈμ΄μ μμΈ 118
3.3. νκΈ°λ²κ³Ό μ‘°μ΄λ²μ μ μΈμνμ§ λͺ»ν μ€λ₯ 122
3.4. κ΅μ‘κ³Όμ μ μν₯μ μν μ€λ₯ 126
3.5. κΈ°ν 128
β
£. μ‘°μ΄λ²μ νμ©ν μΈλμ΄ κ΅μ‘μ μ€μ 130
1. νκ΅μ΄ μΈλμ΄ κ΅μ‘μ λͺ©μ κ³Ό λͺ©ν 130
2. νκ΅μ΄ μΈλμ΄ κ΅μ‘μ λ΄μ© 132
2.1. μ‘°μ΄λ² λ° μΈλμ΄ μ‘°μ΄ μ νμ λν μ΄ν΄ 136
2.2. μ‘°μ΄λ² μ§μμ νμ©ν μΈλμ΄μ ννμ νΉμ§ λΆμ 137
2.3. μΌλΆ μΈλμ΄ νκΈ°λ²μ λν κ°μ‘° 138
2.4. μΈλμ΄ μλ―Έμ λν΄ μ€λͺ
141
2.5. μλ‘μ΄ λ¨μ΄μ μμ± 144
3. νκ΅μ΄ μΈλμ΄ κ΅μ‘νμ΅μ λ°©λ² 145
3.1. μΈμκ³Ό νꡬλ₯Ό ν΅ν κ΅μ‘ λ°©λ² 145
3.2. μΈλμ΄ μ΄νμ§λ μμ
λͺ¨ν μ μ 147
4. μΈλμ΄ κ΅μ‘νμ΅ ν¨κ³Ό κ²μ¦ 159
4.1. μ€ν λ΄μ© λ° μ°Έμ¬μ μ μ 160
4.2. μ€ν λꡬ 161
4.3. μ€ν κ²°κ³Ό λΆμ 164
β
€. κ²°λ‘ 174
β»μ°Έκ³ λ¬Έν 177
β»λΆλ‘ 185
β»ABSTRACT 197Maste
Properties of the highβspin heme of MauG are altered by binding of preMADH at the protein surface 40 Γ away
The diheme enzyme MauG catalyzes oxidative post-translational modifications of a protein substrate, precursor protein of methylamine dehydrogenase (preMADH), that binds to the surface of MauG. The high-spin heme iron of MauG is located 40 Γ
from preMADH. The ferric heme is an equilibrium of five- and six-coordinate states. PreMADH binding increases the proportion of five-coordinate heme three-fold. On reaction of MauG with H2O2 both hemes become FeIV. In the absence of preMADH the hemes autoreduce to ferric in a multistep process involving multiple electron and proton transfers. Binding of preMADH in the absence of catalysis alters the mechanism of autoreduction of the ferryl heme. Thus, substrate binding alters the environment in the distal heme pocket of the high-spin heme over very long distance
Properties Of The High-Spin Heme Of Maug Are Altered By Binding Of Premadh At The Protein Surface 40 Γ Away
The diheme enzyme MauG catalyzes oxidative post-translational modifications of a protein substrate, precursor protein of methylamine dehydrogenase (preMADH), that binds to the surface of MauG. The high-spin heme iron of MauG is located 40 Γ
from preMADH. The ferric heme is an equilibrium of five- and six-coordinate states. PreMADH binding increases the proportion of five-coordinate heme three-fold. On reaction of MauG with H2O2 both hemes become FeIV. In the absence of preMADH the hemes autoreduce to ferric in a multistep process involving multiple electron and proton transfers. Binding of preMADH in the absence of catalysis alters the mechanism of autoreduction of the ferryl heme. Thus, substrate binding alters the environment in the distal heme pocket of the high-spin heme over very long distance
A T67A Mutation In The Proximal Pocket Of The High-Spin Heme Of Maug Stabilizes Formation Of A Mixed-Valent Fe\u3csup\u3eIi\u3c/sup\u3e/Fe\u3csup\u3eIii\u3c/sup\u3e State And Enhances Charge Resonance Stabilization Of The Bis-Fe\u3csup\u3eIv\u3c/sup\u3e State
The diheme enzyme MauG catalyzes a six-electron oxidation required for posttranslational modification of a precursor of methylamine dehydrogenase (preMADH) to complete the biosynthesis of its protein-derived tryptophan tryptophylquinone (TTQ) cofactor. One heme is low-spin with ligands provided by His205 and Tyr294, and the other is high-spin with a ligand provided by His35. The side chain methyl groups of Thr67 and Leu70 are positioned at a distance of 3.4 Γ
on either side of His35, maintaining a hydrophobic environment in the proximal pocket of the high-spin heme and restricting the movement of this ligand. Mutation of Thr67 to Ala in the proximal pocket of the high-spin heme prevented reduction of the low-spin heme by dithionite, yielding a mixed-valent state. The mutation also enhanced the stabilization of the charge-resonance-transition of the high-valent bis-FeIV state that is generated by addition of H2O2. The rates of electron transfer from TTQ biosynthetic intermediates to the high-valent form of T67A MauG were similar to that of wild-type MauG. These results are compared to those previously reported for mutation of residues in the distal pocket of the high-spin heme that also affected the redox properties and charge resonance transition stabilization of the high-valent state of the hemes. However, given the position of residue 67, the structure of the variant protein and the physical nature of the T67A mutation, the basis for the effects of the T67A mutation must be different from those of the mutations of the residues in the distal heme pocket
HYDROLOGICAL PROCESSES
Detecting water yield variability due to the small proportional land use and land cover changes in a watershed on the Loess Plateau, Chin