Base de dados : MEDLINE
Pesquisa : G02.282 [Categoria DeCS]
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  1 / 36149 MEDLINE  
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[PMID]:28471375
[Au] Autor:Zhao M; Shao GK; Huang DD; Lv XX; Guo DS
[Ad] Endereço:College of Chemistry, Chemical Engineering and Materials Science, Collaborative Innovation Center of Functionalized Probes for Chemical Imaging in Universities of Shandong, Shandong Normal University, Jinan 250014, China. chmeizhao@163.com.
[Ti] Título:Synthesis, Crystal Structures and Properties of Ferrocenyl Bis-Amide Derivatives Yielded via the Ugi Four-Component Reaction.
[So] Source:Molecules;22(5), 2017 May 04.
[Is] ISSN:1420-3049
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Ten ferrocenyl bis-amide derivatives were successfully synthesized via the Ugi four-component reaction by treating ferrocenecarboxylic acid with diverse aldehydes, amines, and isocyanides in methanol solution. Their chemical structures were fully characterized by IR, NMR, HR-MS, and X-ray diffraction analyses. They feature unique molecular morphologies and create a 14-membered ring motif in the centro-symmetric dimers generated in the solid state. Moreover, the electrochemical behavior of these ferrocenyl bis-amides was assessed by cyclic voltammetry.
[Mh] Termos MeSH primário: Amidas/química
Compostos Ferrosos/química
[Mh] Termos MeSH secundário: Amidas/síntese química
Cristalografia por Raios X
Técnicas Eletroquímicas
Ligações de Hidrogênio
Espectroscopia de Ressonância Magnética
Espectrometria de Massas
Espectrofotometria Infravermelho
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amides); 0 (Ferrous Compounds); 1271-42-7 (ferrocenecarboxylic acid)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE


  2 / 36149 MEDLINE  
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[PMID]:28463369
[Au] Autor:Ndagi U; Mhlongo NN; Soliman ME
[Ad] Endereço:Molecular Modelling and Drug Design Research Group, School of Health Sciences, University of KwaZulu-Natal, Westville, Durban 4000, South Africa. soliman@ukzn.ac.za.
[Ti] Título:The impact of Thr91 mutation on c-Src resistance to UM-164: molecular dynamics study revealed a new opportunity for drug design.
[So] Source:Mol Biosyst;13(6):1157-1171, 2017 May 30.
[Is] ISSN:1742-2051
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The emergence of a drug resistant non-receptor tyrosine kinase (c-Src) in triple-negative breast cancer (TNBC) remains a prime concern in relation to the burden of TNBC among people living with breast cancer and drug development. Thr91 mutation was found to induce a complete loss of protein conformation required for drug fitness. Herein, we provide the first account of the molecular impact of the Thr91 mutation on c-Src resistance to experimental drug UM-164 using various computational approaches, namely molecular dynamics simulation, principal component analysis (PCA), dynamic cross-correlation matrices (DCCM) analysis, hydrogen bond occupancy, thermodynamics calculation, ligand-residue interaction and residue interaction networks (RINs). Findings from this study revealed that Thr91 mutation leads to a steric conflict between UM-164 and the side chain of methionine (Met91); this mutation distorts the UM-164 optimum orientation on the conformational space of mutant c-Src compared to the wild-type; decreases hydrogen bond formation between the residues in the mutant protein structure; decreases the UM-164 binding energy in the mutant by -13.416 kcal mol ; reduces the residue correlation in the mutant protein structure; induces a change in the overall protein structure conformation from an inactive to active conformation; and distorts the ligand atomic interaction network and the residue interaction network. This report provides important insights that will assist in the further design of novel dual kinase inhibitors to minimise the chances of drug resistance in triple negative breast cancer.
[Mh] Termos MeSH primário: Simulação de Dinâmica Molecular
Neoplasias de Mama Triplo Negativas/genética
[Mh] Termos MeSH secundário: Desenho de Drogas
Farmacorresistência Viral/genética
Seres Humanos
Ligações de Hidrogênio
Mutação
Análise de Componente Principal
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE
[do] DOI:10.1039/c6mb00848h


  3 / 36149 MEDLINE  
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[PMID]:28453010
[Au] Autor:Sethi S; Ooe M; Sakamoto T; Fujimoto K
[Ad] Endereço:School of Materials Science, Japan Advanced Institute of Science and Technology, 1-1 Asahidai, Nomi, Ishikawa 923-1292, Japan. kenzo@jaist.ac.jp.
[Ti] Título:Effect of nucleobase change on cytosine deamination through DNA photo-cross-linking reaction via 3-cyanovinylcarbazole nucleoside.
[So] Source:Mol Biosyst;13(6):1152-1156, 2017 Jun 01.
[Is] ISSN:1742-2051
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Photo-chemical deamination of cytosine using 3-cyanovinylcarbazole nucleoside ( K) mediated photo-cross-linking is a technique for site-directed mutagenesis. Using this technique in vivo requires the elimination of a high-temperature incubation step; instead, incubation should be carried out under physiological conditions. To improve the reactivity of K mediated photo-cross-link induced deamination of cytosine under physiological conditions, an evaluation of base pairing in cytosine was carried out with respect to its deamination. Guanine was replaced with 4 different counter bases (inosine, 2-aminopurine, 5-nitroindole, and nebularine), showing distinct hydrogen bonding patterns with target cytosine, which was incorporated at the -1 position with respect to K in the K-modified photo-responsive oligodeoxyribonucleotides to ascertain the role of hydrogen bonding in deamination under physiological conditions. Among the counter bases, inosine showed the highest acceleration towards the photo-induced deamination reaction.
[Mh] Termos MeSH primário: Citosina/química
DNA/química
Guanina/química
Nucleosídeos/química
[Mh] Termos MeSH secundário: 2-Aminopurina/química
Pareamento de Bases
Desaminação
Ligações de Hidrogênio
Indóis/química
Estrutura Molecular
Mutagênese Sítio-Dirigida
Oligodesoxirribonucleotídeos/química
Nucleosídeos de Purina/química
Ribonucleosídeos/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Indoles); 0 (Nucleosides); 0 (Oligodeoxyribonucleotides); 0 (Purine Nucleosides); 0 (Ribonucleosides); 452-06-2 (2-Aminopurine); 5Z93L87A1R (Guanine); 8J337D1HZY (Cytosine); 9007-49-2 (DNA); B8B604PS4P (nebularine); O2BHX6EDBN (5-nitroindole)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170429
[St] Status:MEDLINE
[do] DOI:10.1039/c7mb00082k


  4 / 36149 MEDLINE  
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[PMID]:28449057
[Au] Autor:Schumacher MA; Zeng W; Findlay KC; Buttner MJ; Brennan RG; Tschowri N
[Ad] Endereço:Department of Biochemistry, Duke University School of Medicine, Durham, NC 27701, USA.
[Ti] Título:The Streptomyces master regulator BldD binds c-di-GMP sequentially to create a functional BldD2-(c-di-GMP)4 complex.
[So] Source:Nucleic Acids Res;45(11):6923-6933, 2017 Jun 20.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Streptomyces are ubiquitous soil bacteria that undergo a complex developmental transition coinciding with their production of antibiotics. This transition is controlled by binding of a novel tetrameric form of the second messenger, 3΄-5΄ cyclic diguanylic acid (c-di-GMP) to the master repressor, BldD. In all domains of life, nucleotide-based second messengers allow a rapid integration of external and internal signals into regulatory pathways that control cellular responses to changing conditions. c-di-GMP can assume alternative oligomeric states to effect different functions, binding to effector proteins as monomers, intercalated dimers or, uniquely in the case of BldD, as a tetramer. However, at physiological concentrations c-di-GMP is a monomer and little is known about how higher oligomeric complexes assemble on effector proteins and if intermediates in assembly pathways have regulatory significance. Here, we show that c-di-GMP binds BldD using an ordered, sequential mechanism and that BldD function necessitates the assembly of the BldD2-(c-di-GMP)4 complex.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
GMP Cíclico/análogos & derivados
Proteínas Repressoras/química
Streptomyces
[Mh] Termos MeSH secundário: Sítios de Ligação
Cristalografia por Raios X
GMP Cíclico/química
Ligações de Hidrogênio
Modelos Moleculares
Ligação Proteica
Domínios Proteicos
Estabilidade Proteica
Estrutura Quaternária de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Repressor Proteins); 61093-23-0 (bis(3',5')-cyclic diguanylic acid); H2D2X058MU (Cyclic GMP)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:180307
[Lr] Data última revisão:
180307
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170428
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx287


  5 / 36149 MEDLINE  
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[PMID]:29349451
[Au] Autor:Habka S; Sohn WY; Vaquero-Vara V; Géléoc M; Tardivel B; Brenner V; Gloaguen E; Mons M
[Ad] Endereço:LIDYL, CEA, CNRS, Université Paris Saclay, CEA Saclay, Bât 522, 91191 Gif-sur-Yvette, France. michel.mons@cea.fr.
[Ti] Título:On the turn-inducing properties of asparagine: the structuring role of the amide side chain, from isolated model peptides to crystallized proteins.
[So] Source:Phys Chem Chem Phys;20(5):3411-3423, 2018 Jan 31.
[Is] ISSN:1463-9084
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Asparagine (Asn) is a powerful turn-inducer residue, with a large propensity to occupy the second position in the central region of ß-turns of proteins. The present work aims at investigating the role of a local anchoring between the Asn side chain and the main chain in this remarkable property. For this purpose, the H-bonding patterns of an asparagine residue in an isolated protein chain fragment forming a γ- or a ß-turn have been determined using IR/UV double resonance gas phase spectroscopy on laser-desorbed, jet-cooled short models in conjunction with relevant quantum chemistry calculations. These gas phase data provide evidence for an original double anchoring linking the Asn primary amide side chain (SC), which adopts a gauche+ rotameric form, to its main chain (MC) local environment. From both IR spectroscopic evidence (H-bond induced red shifts) and quantum chemistry, Asn SC is found to behave as a stronger H-bond acceptor than donor, resulting in stronger MC→SC H-bonds than SC→MC ones. These gas phase structural data, relevant to a hydrophobic environment, have been used as a reference to assess the anchoring taking place in high resolution crystallized proteins of the Protein Data Bank. This approach reveals that, when the SC adopts a gauche+ orientation, the stronger MC→SC bonds are preserved in many cases whereas the SC→MC bonds are always disrupted, in qualitative agreement with the gas phase ranking of these interactions. Most interestingly, when Asn occupies the second position of central part of a ß-turn (i.e., the very turn-inducer position), the MC→SC H-bonds are also disrupted and replaced by a water-mediated SC to MC anchoring. Owing to the specific features of the hydrated Asn side chain, we propose that it could be a turn precursor structure, able to facilitate turn formation in the early events of the folding process.
[Mh] Termos MeSH primário: Asparagina/química
Peptídeos/química
[Mh] Termos MeSH secundário: Amidas/química
Gases/química
Ligações de Hidrogênio
Estrutura Secundária de Proteína
Teoria Quântica
Espectrofotometria Infravermelho
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amides); 0 (Gases); 0 (Peptides); 7006-34-0 (Asparagine)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180120
[St] Status:MEDLINE
[do] DOI:10.1039/c7cp07605c


  6 / 36149 MEDLINE  
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[PMID]:29345270
[Au] Autor:Chawla M; Autiero I; Oliva R; Cavallo L
[Ad] Endereço:King Abdullah University of Science and Technology (KAUST), Physical Sciences and Engineering Division, Kaust Catalysis Center, Thuwal 23955-6900, Saudi Arabia. mohitchawla.bt@gmail.com luigi.cavallo@kaust.edu.sa.
[Ti] Título:Energetics and dynamics of the non-natural fluorescent 4AP:DAP base pair.
[So] Source:Phys Chem Chem Phys;20(5):3699-3709, 2018 Jan 31.
[Is] ISSN:1463-9084
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The fluorescent non-natural 4-aminophthalimide (4AP) base, when paired to the complementary 2,4-diaminopyrimidine (DAP) nucleobase, is accommodated in a B-DNA duplex being efficiently recognized and incorporated by DNA polymerases. To complement the experimental studies and rationalize the impact of the above non-natural bases on the structure, stability and dynamics of nucleic acid structures, we performed quantum mechanics (QM) calculations along with classical molecular dynamics (MD) simulations. QM calculations were initially focused on the geometry and energetics of the 4AP:DAP non-natural pair and of H-bonded base pairs between 4AP and all the natural bases in their classical Watson-Crick geometries. The QM calculations indicate that the 4AP:DAP pair, despite the fact that it can form 3 H-bonds in a classic Watson-Crick geometry, has a stability comparable to the A:T pair. Then, we extended the study to reverse Watson-Crick geometries, characteristic of parallel strands. MD simulations were carried out on two 13-mer DNA duplexes, featuring a central 4AP:DAP or A:T pair, respectively. No major structural deformation of the duplex was observed during the MD simulation. Snapshots from the MD simulations were subjected to QM calculations to investigate the 4AP:DAP interaction energy when embedded into a duplex structure, and to investigate the impact of the two non-natural bases on the stacking interactions with adjacent bases in the DNA duplex. We found a slight increase in stacking interactions involving the 4AP:DAP pair, counterbalanced by a moderate decrease in H-bonding interactions of the 4AP:DAP and of the adjacent base pairs in the duplex. The results of our study are in agreement with experimental data and complement them by providing an insight into which factors contribute positively and which factors contribute negatively to the structural compatibility of the fluorescent 4AP:DAP pair with a B-DNA structure.
[Mh] Termos MeSH primário: Ftalimidas/química
Pirimidinas/química
[Mh] Termos MeSH secundário: Pareamento de Bases
DNA de Forma B/química
Ligações de Hidrogênio
Conformação Molecular
Simulação de Dinâmica Molecular
Ftalimidas/metabolismo
Pirimidinas/metabolismo
Teoria Quântica
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (4-aminophthalimide); 0 (DNA, B-Form); 0 (Phthalimides); 0 (Pyrimidines); 156-81-0 (2,4-diaminopyrimidine)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180119
[St] Status:MEDLINE
[do] DOI:10.1039/c7cp07400j


  7 / 36149 MEDLINE  
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[PMID]:29333856
[Au] Autor:Xie Y; Zhu X; Li Y; Wang C
[Ad] Endereço:School of Food Science and Technology, Henan University of Technology , Zhengzhou, Henan 450001, People's Republic of China.
[Ti] Título:Analysis of the pH-Dependent Fe(III) Ion Chelating Activity of Anthocyanin Extracted from Black Soybean [Glycine max (L.) Merr.] Coats.
[So] Source:J Agric Food Chem;66(5):1131-1139, 2018 Feb 07.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Fe(III) chelating activity of anthocyanin extracted from black soybean coats was investigated at pH 3.0, 5.0, 6.5, 7.0, and 7.4 with fluorescence spectroscopy and microscale thermophoresis (MST). Cyanidin-3-glucoside (C3G) was determined to be 98% of the total anthocyanin by high-performance liquid chromatography. The binding affinity (K ) exhibited significant pH-dependent behavior: K was 9.7167 × 10 , 1.0837 × 10 , 1.4284 × 10 , 5.4550 × 10 , and 3.0269 × 10 M at pH 3.0, 5.0, 6.5, 7.0, and 7.4, respectively (p < 0.05). The MST data showed that ΔG < 0 and ΔH < 0, demonstrating that chelation is spontaneous and exothermic. Because both ΔH and ΔS < 0, the chelation involves hydrogen bonds and/or van der Waals forces for pH 3.0, 5.0, and 6.5. Electrostatic interactions contributed to chelation at pH 7.0 and 7.4 with ΔH < 0 and ΔS > 0. With the formation of chelates, C3G improved the solubility of Fe(III) at pH 6.5, 7.0, and 7.4 to enhance the ferric ion bioavailability, except for aggregation observed at pH 5.0.
[Mh] Termos MeSH primário: Antocianinas/química
Antocianinas/isolamento & purificação
Compostos Férricos/química
Quelantes de Ferro/química
Feijão de Soja/química
[Mh] Termos MeSH secundário: Disponibilidade Biológica
Ligações de Hidrogênio
Concentração de Íons de Hidrogênio
Solubilidade
Espectrometria de Fluorescência
Eletricidade Estática
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anthocyanins); 0 (Ferric Compounds); 0 (Iron Chelating Agents)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180116
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b04719


  8 / 36149 MEDLINE  
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[PMID]:29297909
[Au] Autor:Katayama K; Furutani Y; Iwaki M; Fukuda T; Imai H; Kandori H
[Ad] Endereço:Department of Life Science and Applied Chemistry, Nagoya Institute of Technology, Showa-ku, Nagoya 466-8555, Japan. kandori@nitech.ac.jp.
[Ti] Título:"In situ" observation of the role of chloride ion binding to monkey green sensitive visual pigment by ATR-FTIR spectroscopy.
[So] Source:Phys Chem Chem Phys;20(5):3381-3387, 2018 Jan 31.
[Is] ISSN:1463-9084
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Long-wavelength-sensitive (LWS) pigment possesses a chloride binding site in its protein moiety. The binding of chloride alters the absorption spectra of LWS; this is known as the chloride effect. Although the two amino acid substitutions of His197 and Lys200 influence the chloride effect, the molecular mechanism of chloride binding, which underlies the spectral tuning, has yet to be clarified. In this study, we applied ATR-FTIR spectroscopy to monkey green (MG) pigment to gain structural information of the chloride binding site. The results suggest that chloride binding stabilizes the ß-sheet structure on the extracellular side loop with perturbation of the retinal polyene chain, promotes a hydrogen bonding exchange with the hydroxyl group of Tyr, and alters the protonation state of carboxylate. Combining with the results of the binding analyses of various anions (Br , I and NO ), our findings suggest that the anion binding pocket is organized for only Cl (or Br ) to stabilize conformation around the retinal chromophore, which is functionally relevant with absorbing long wavelength light.
[Mh] Termos MeSH primário: Cloretos/química
Pigmentos da Retina/química
[Mh] Termos MeSH secundário: Animais
Ânions/química
Sítios de Ligação
Cercopithecus aethiops
Cloretos/metabolismo
Células HEK293
Seres Humanos
Ligações de Hidrogênio
Estrutura Secundária de Proteína
Proteínas Recombinantes/biossíntese
Proteínas Recombinantes/química
Proteínas Recombinantes/isolamento & purificação
Pigmentos da Retina/genética
Pigmentos da Retina/metabolismo
Espectroscopia de Infravermelho com Transformada de Fourier
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anions); 0 (Chlorides); 0 (Recombinant Proteins); 0 (Retinal Pigments)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180104
[St] Status:MEDLINE
[do] DOI:10.1039/c7cp07277e


  9 / 36149 MEDLINE  
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[PMID]:29297914
[Au] Autor:Swadling JB; Ishii K; Tahara T; Kitao A
[Ad] Endereço:School of Life Science and Technology, Tokyo Institute of Technology, 2-12-1 Ookayama, M6-13, Meguro, Tokyo 152-8550, Japan. akitao@bio.titech.ac.jp.
[Ti] Título:Origins of biological function in DNA and RNA hairpin loop motifs from replica exchange molecular dynamics simulation.
[So] Source:Phys Chem Chem Phys;20(5):2990-3001, 2018 Jan 31.
[Is] ISSN:1463-9084
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Deoxyribonucleic acid (DNA) and ribonucleic acid (RNA) have remarkably similar chemical structures, but despite this, they play significantly different roles in modern biology. In this article, we explore the possible conformations of DNA and RNA hairpins to better understand the fundamental differences in structure formation and stability. We use large parallel temperature replica exchange molecular dynamics ensembles to sample the full conformational landscape of these hairpin molecules so that we can identify the stable structures formed by the hairpin sequence. Our simulations show RNA adopts a narrower distribution of folded structures compared to DNA at room temperature, which forms both hairpins and many unfolded conformations. RNA is capable of forming twice as many hydrogen bonds than DNA which results in a higher melting temperature. We see that local chemical differences lead to emergent molecular properties such as increased persistence length in RNA that is weakly temperature dependant. These discoveries provide fundamental insight into how RNA forms complex folded tertiary structures which confer enzymatic-like function in ribozymes, whereas DNA retains structural motifs in order to facilitate function such as translation of sequence.
[Mh] Termos MeSH primário: DNA/química
Simulação de Dinâmica Molecular
RNA/química
[Mh] Termos MeSH secundário: Transferência Ressonante de Energia de Fluorescência
Ligações de Hidrogênio
Sequências Repetidas Invertidas/genética
Conformação de Ácido Nucleico
Termodinâmica
Temperatura de Transição
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
63231-63-0 (RNA); 9007-49-2 (DNA)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180104
[St] Status:MEDLINE
[do] DOI:10.1039/c7cp06355e


  10 / 36149 MEDLINE  
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[PMID]:29260810
[Au] Autor:Chang S; Mizuno M; Ishikawa H; Mizutani Y
[Ad] Endereço:Department of Chemistry, Graduate School of Science, Osaka University, 1-1 Machikaneyama, Toyonaka, Osaka 560-0043, Japan. mztn@chem.sci.osaka-u.ac.jp.
[Ti] Título:Tertiary dynamics of human adult hemoglobin fixed in R and T quaternary structures.
[So] Source:Phys Chem Chem Phys;20(5):3363-3372, 2018 Jan 31.
[Is] ISSN:1463-9084
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Protein dynamics of human adult hemoglobin and its mutants restricted in R and T quaternary states following ligand photolysis were studied by time-resolved resonance Raman spectroscopy. In the time-resolved spectra, we observed spectral changes of in-plane stretching modes of heme and the iron-histidine stretching mode of the Fe-His bond for all the hemoglobin samples. The ßD99N mutant, which adopts the R state in both the ligand-bound and the deoxy forms, showed similar temporal behaviors in time-resolved resonance Raman spectra as wild-type recombinant hemoglobin until 10 µs, consistent with the fact that the mutant undergoes only the tertiary structural changes in the R state. The ßN102T mutant, which adopts the T state in both the ligand-bound and the deoxy forms, showed much slower tertiary structural changes, suggesting that the EF helical motion is decelerated by the change of the intersubunit interactions. The present data indicate that the allosteric kinetic response between the interhelical hydrogen bonds of the EF helices and the intersubunit hydrogen bonds is bidirectional. The implications of these results for understanding the allosteric pathway of Hb are discussed in detail.
[Mh] Termos MeSH primário: Hemoglobinas/química
[Mh] Termos MeSH secundário: Adulto
Heme/química
Heme/metabolismo
Hemoglobinas/genética
Hemoglobinas/metabolismo
Histidina/química
Histidina/metabolismo
Seres Humanos
Ligações de Hidrogênio
Mutagênese Sítio-Dirigida
Estrutura Quaternária de Proteína
Proteínas Recombinantes/biossíntese
Proteínas Recombinantes/química
Proteínas Recombinantes/isolamento & purificação
Análise Espectral Raman
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Hemoglobins); 0 (Recombinant Proteins); 42VZT0U6YR (Heme); 4QD397987E (Histidine)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171221
[St] Status:MEDLINE
[do] DOI:10.1039/c7cp06287g



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