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CHEMISTRY (593 journals)                  1 2 3 | Last

Showing 1 - 200 of 735 Journals sorted alphabetically
2D Materials     Hybrid Journal   (Followers: 8)
Accreditation and Quality Assurance: Journal for Quality, Comparability and Reliability in Chemical Measurement     Hybrid Journal   (Followers: 26)
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Acta Metallurgica Sinica (English Letters)     Hybrid Journal   (Followers: 5)
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adhäsion KLEBEN & DICHTEN     Hybrid Journal   (Followers: 5)
Adhesion Adhesives & Sealants     Hybrid Journal   (Followers: 7)
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African Journal of Bacteriology Research     Open Access  
African Journal of Chemical Education     Open Access   (Followers: 2)
African Journal of Pure and Applied Chemistry     Open Access   (Followers: 7)
Agrokémia és Talajtan     Full-text available via subscription   (Followers: 2)
Alkaloids: Chemical and Biological Perspectives     Full-text available via subscription   (Followers: 3)
AMB Express     Open Access   (Followers: 1)
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American Journal of Biochemistry and Molecular Biology     Open Access   (Followers: 14)
American Journal of Chemistry     Open Access   (Followers: 26)
American Journal of Plant Physiology     Open Access   (Followers: 14)
American Mineralogist     Hybrid Journal   (Followers: 14)
Analyst     Full-text available via subscription   (Followers: 40)
Angewandte Chemie     Hybrid Journal   (Followers: 219)
Angewandte Chemie International Edition     Hybrid Journal   (Followers: 212)
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Arabian Journal of Chemistry     Open Access   (Followers: 6)
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Atomization and Sprays     Full-text available via subscription   (Followers: 4)
Australian Journal of Chemistry     Hybrid Journal   (Followers: 7)
Autophagy     Hybrid Journal   (Followers: 2)
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Bioorganic & Medicinal Chemistry Letters     Hybrid Journal   (Followers: 96)
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Bitácora Digital     Open Access  
Boletin de la Sociedad Chilena de Quimica     Open Access  
Bulletin of the Chemical Society of Ethiopia     Open Access   (Followers: 2)
Bulletin of the Chemical Society of Japan     Full-text available via subscription   (Followers: 24)
Bulletin of the Korean Chemical Society     Hybrid Journal   (Followers: 1)
C - Journal of Carbon Research     Open Access   (Followers: 3)
Cakra Kimia (Indonesian E-Journal of Applied Chemistry)     Open Access  
Canadian Association of Radiologists Journal     Full-text available via subscription   (Followers: 3)
Canadian Journal of Chemistry     Hybrid Journal   (Followers: 10)
Canadian Mineralogist     Full-text available via subscription   (Followers: 3)
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Catalysis for Sustainable Energy     Open Access   (Followers: 7)
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Catalysis Surveys from Asia     Hybrid Journal   (Followers: 3)
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Chemical and Engineering News     Free   (Followers: 13)
Chemical Bulletin of Kazakh National University     Open Access  
Chemical Communications     Full-text available via subscription   (Followers: 71)
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Chemical Reviews     Full-text available via subscription   (Followers: 174)
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Chemical Technology     Open Access   (Followers: 16)
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Chemical Week     Full-text available via subscription   (Followers: 8)
Chemie in Unserer Zeit     Hybrid Journal   (Followers: 57)
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Chemistry & Industry     Hybrid Journal   (Followers: 5)
Chemistry - A European Journal     Hybrid Journal   (Followers: 142)
Chemistry - An Asian Journal     Hybrid Journal   (Followers: 15)
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Chemistry Central Journal     Open Access   (Followers: 4)
Chemistry Education Research and Practice     Free   (Followers: 5)
Chemistry in Education     Open Access   (Followers: 9)
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Chemistry Letters     Full-text available via subscription   (Followers: 45)
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Chemistry of Natural Compounds     Hybrid Journal   (Followers: 9)
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Chemkon - Chemie Konkret, Forum Fuer Unterricht Und Didaktik     Hybrid Journal  
Chemoecology     Hybrid Journal   (Followers: 3)
Chemometrics and Intelligent Laboratory Systems     Hybrid Journal   (Followers: 15)
Chemosensors     Open Access  
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ChemTexts     Hybrid Journal  
CHIMIA International Journal for Chemistry     Full-text available via subscription   (Followers: 2)
Chinese Journal of Chemistry     Hybrid Journal   (Followers: 6)
Chinese Journal of Polymer Science     Hybrid Journal   (Followers: 10)
Chromatographia     Hybrid Journal   (Followers: 24)
Clay Minerals     Full-text available via subscription   (Followers: 10)
Cogent Chemistry     Open Access  
Colloid and Interface Science Communications     Open Access  
Colloid and Polymer Science     Hybrid Journal   (Followers: 10)
Colloids and Surfaces B: Biointerfaces     Hybrid Journal   (Followers: 7)
Combinatorial Chemistry & High Throughput Screening     Hybrid Journal   (Followers: 4)
Combustion Science and Technology     Hybrid Journal   (Followers: 18)
Comments on Inorganic Chemistry: A Journal of Critical Discussion of the Current Literature     Hybrid Journal   (Followers: 2)
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        1 2 3 | Last

Journal Cover Biomolecular NMR Assignments
  [SJR: 0.325]   [H-I: 10]   [3 followers]  Follow
   Hybrid Journal Hybrid journal (It can contain Open Access articles)
   ISSN (Print) 1874-2718 - ISSN (Online) 1874-270X
   Published by Springer-Verlag Homepage  [2353 journals]
  • Chemical shift assignments of the first and second RRMs of Nrd1, a fission
           yeast MAPK-target RNA binding protein
    • Authors: Ayaho Kobayashi; Teppei Kanaba; Ryosuke Satoh; Yutaka Ito; Reiko Sugiura; Masaki Mishima
      Pages: 123 - 126
      Abstract: Abstract Negative regulator differentiation 1 (Nrd1), a fission yeast RNA binding protein, modulates cytokinesis and sexual development and contributes to stress granule formation in response to environmental stresses. Nrd1 comprises four RRM domains and binds and stabilizes Cdc4 mRNA that encodes the myosin II light chain. Nrd1 binds the Cpc2 fission-yeast RACK1 homolog, and the interaction promotes Nrd1 localization to stress granules. Interestingly, Pmk1 mitogen-activated protein kinase phosphorylates Thr40 in the unstructured N-terminal region and Thr126 in the first RRM domain of Nrd1. Phosphorylation significantly reduces RNA-binding activity and likely modulates Nrd1 function. To reveal the relationship between the structure and function of Nrd1 and how phosphorylation affects structure, we used heteronuclear NMR techniques to investigate the three-dimensional structure of Nrd1. Here we report the 1H, 13C, and 15N resonance assignments of RRM1–RRM2 (residues 108–284) comprising the first and second RRMs obtained using heteronuclear NMR techniques. Secondary structures derived from the chemical shifts are reported. These data should contribute to the understanding of the three-dimensional structure of the RRM1–RRM2 region of Nrd1 and the perturbation caused by phosphorylation.
      PubDate: 2017-10-01
      DOI: 10.1007/s12104-017-9731-1
      Issue No: Vol. 11, No. 2 (2017)
  • Chemical shift assignments of the connexin37 carboxyl terminal domain
    • Authors: Hanjun Li; Gaelle Spagnol; Tasha K. Pontifex; Janis M. Burt; Paul L. Sorgen
      Pages: 137 - 141
      Abstract: Abstract Connexin37 (Cx37) is a gap junction protein involved in cell-to-cell communication in the vasculature and other tissues. Cx37 suppresses proliferation of vascular cells involved in tissue development and repair in vivo, as well as tumor cells. Global deletion of Cx37 in mice leads to enhanced vasculogenesis in development, as well as collateralgenesis and angiogenesis in response to injury, which together support improved tissue remodeling and recovery following ischemic injury. Here we report the 1H, 15N, and 13C resonance assignments for an important regulatory domain of Cx37, the carboxyl terminus (CT; C233-V333). The predicted secondary structure of the Cx37CT domain based on the chemical shifts is that of an intrinsically disordered protein. In the 1H–15N HSQC, N-terminal residues S254-Y259 displayed a second weaker peak and residues E261-Y266 had significant line broadening. These residues are flanked by prolines (P250, P258, P260, and P268), suggesting proline cis–trans isomerization. Overall, these assignments will be useful for identifying the binding sites for intra- and inter-molecular interactions that affect Cx37 channel activity.
      PubDate: 2017-10-01
      DOI: 10.1007/s12104-017-9735-x
      Issue No: Vol. 11, No. 2 (2017)
  • Sequence-specific backbone resonance assignments and microsecond timescale
           molecular dynamics simulation of human eosinophil-derived neurotoxin
    • Authors: Donald Gagné; Chitra Narayanan; Khushboo Bafna; Laurie-Anne Charest; Pratul K. Agarwal; Nicolas Doucet
      Pages: 143 - 149
      Abstract: Abstract Eight active canonical members of the pancreatic-like ribonuclease A (RNase A) superfamily have been identified in human. All structural homologs share similar RNA-degrading functions, while also cumulating other various biological activities in different tissues. The functional homologs eosinophil-derived neurotoxin (EDN, or RNase 2) and eosinophil cationic protein (ECP, or RNase 3) are known to be expressed and secreted by eosinophils in response to infection, and have thus been postulated to play an important role in host defense and inflammatory response. We recently initiated the biophysical and dynamical investigation of several vertebrate RNase homologs and observed that clustering residue dynamics appear to be linked with the phylogeny and biological specificity of several members. Here we report the 1H, 13C and 15N backbone resonance assignments of human EDN (RNase 2) and its molecular dynamics simulation on the microsecond timescale, providing means to pursue this comparative atomic-scale functional and dynamical analysis by NMR and computation over multiple time frames.
      PubDate: 2017-10-01
      DOI: 10.1007/s12104-017-9736-9
      Issue No: Vol. 11, No. 2 (2017)
  • Backbone assignments for the SPOUT methyltransferase MTT Tm , a knotted
           protein from Thermotoga maritima
    • Authors: David J. Burban; Patricia A. Jennings
      Pages: 151 - 154
      Abstract: Abstract The SPOUT family of methyltransferase proteins is noted for containing a deep trefoil knot in their defining backbone fold. This unique fold is of high interest for furthering the understanding of knots in proteins. Here, we report the 1H, 13C, 15N assignments for MTT Tm , a canonical member of the SPOUT family. This protein is unique, as it is one of the smallest members of the family, making it an ideal system for probing the unique properties of the knot. Our present work represents the foundation for further studies into the topology of MTT Tm , and understanding how its structure affects both its folding and function.
      PubDate: 2017-10-01
      DOI: 10.1007/s12104-017-9737-8
      Issue No: Vol. 11, No. 2 (2017)
  • Backbone resonance assignments of the Escherichia coli 62 kDa
           protein, Hsp31
    • Authors: Jihong Kim; Dongwook Choi; Chankyu Park; Kyoung-Seok Ryu
      Pages: 159 - 163
      Abstract: Abstract Dimeric Hsp31 protein was first characterized as a holding chaperone of Escherichia coli (E. coli), and has been suggested as having protease activity due to the presence of a potential catalytic triad, Cys185, His186, and Asp214. However, it has recently been reported that Hsp31 displays a relatively strong glyoxalase III activity that can decompose reactive carbonyl species (methylglyoxal and glyoxal) in the absence of additional cofactor. Hsp31 is a representative member of the DJ-1/ThiJ/PfpI protein superfamily, and the importance of DJ-1 protein in Parkinson’s disease has been well known. The structural flexibility of the long loop region, which encompasses from the P- to the A-domain, is important for the chaperone activity of Hsp31. The backbone chemical shifts (CSs) would be useful for studying the structural changes of Hsp31 that are critical for the holding chaperone activity, and also for deciphering the switching mechanism between the glyoxalase III and the chaperone. Here, we report the backbone CSs (HN, N, CO, Cα, and Cβ) of the deuterated Hsp31 protein (62 kDa). The CS analysis showed that the predicted regions of secondary structures are in good agreement with those observed in the previous crystal structure of Hsp31.
      PubDate: 2017-10-01
      DOI: 10.1007/s12104-017-9739-6
      Issue No: Vol. 11, No. 2 (2017)
  • Near-complete backbone resonance assignments of acid-denatured human
           cytochrome c in dimethylsulfoxide: a prelude to studying interactions with
    • Authors: Andreas Ioannis Karsisiotis; Oliver M. Deacon; Colin Macdonald; Tharin M. A. Blumenschein; Geoffrey R. Moore; Jonathan A. R. Worrall
      Pages: 165 - 168
      Abstract: Abstract Human cytochrome c plays a central role in the mitochondrial electron transfer chain and in the intrinsic apoptosis pathway. Through the interaction with the phospholipid cardiolipin, cytochrome c triggers release of pro-apoptotic factors, including itself, from the mitochondrion into the cytosol of cells undergoing apoptosis. The cytochrome c/cardiolipin complex has been extensively studied through various spectroscopies, most recently with high-field solution and solid-state NMR spectroscopies, but there is no agreement between the various studies on key structural features of cytochrome c in its complex with cardiolipin. In the present study, we report backbone 1H, 13C, 15N resonance assignments of acid-denatured human cytochrome c in the aprotic solvent dimethylsulfoxide. These have led to the assignment of a reference 2D 1H-15N HSQC spectrum in which out of the 99 non-proline residues 87% of the backbone amides are assigned. These assignments are being used in an interrupted H/D exchange strategy to map the binding site of cardiolipin on human cytochrome c.
      PubDate: 2017-10-01
      DOI: 10.1007/s12104-017-9740-0
      Issue No: Vol. 11, No. 2 (2017)
  • Backbone and side-chain resonance assignments for the tmRNA-binding
           protein, SmpB, from Mycobacterium tuberculosis
    • Authors: Juanjuan Yang; Yindi Liu; Zhao Liu; Chun Meng; Donghai Lin
      Pages: 175 - 179
      Abstract: Abstract Small protein B (SmpB) is an essential molecule in trans-translation which is a universal biological pathway for protein synthesis in bacteria. Trans-translation can release stalled ribosomes from defective mRNAs and target tag-protein fragments for degradation, and then restart protein synthesis. The SmpB-tmRNA complex coordinating with other components of the trans-translation system, plays vital roles in Mycobacterium tuberculosis under both stress conditions and non-replicating conditions. Thus, elucidation of molecular details and dynamic properties of the SmpB-tmRNA interaction is a crucial step towards effectively blocking trans-translation process to shorten the duration of tuberculosis treatment. Here, we report resonance assignments for 1H, 13C and 15N of M. tuberculosis SmpB (MtSmpB, spanning residues 4–133) protein determined by a suite of 2D/3D heteronuclear NMR experiments along with predicted the secondary structure.
      PubDate: 2017-10-01
      DOI: 10.1007/s12104-017-9742-y
      Issue No: Vol. 11, No. 2 (2017)
  • 1 H, 13 C, and 15 N backbone chemical shift assignments of 4E-BP1 44–87
           and 4E-BP1 44–87 bound to eIF4E
    • Authors: Naotaka Sekiyama; Andras Boeszoermenyi; Haribabu Arthanari; Gerhard Wagner; Mélissa Léger-Abraham
      Pages: 187 - 191
      Abstract: Abstract The eukaryotic translational initiation factor 4G (eIF4G) interacts with the cap-binding protein eIF4E through a consensus binding motif, Y(X)4LΦ (where X is any amino acid and Φ is a hydrophobic residue). 4E binding proteins (4E-BPs), which also contain a Y(X)4LΦ motif, regulate the eIF4E/eIF4G interaction. The non- or minimally-phosphorylated form of 4E-BP1 binds eIF4E, preventing eIF4E from interacting with eIF4G, thus inhibiting translation initiation. 4EGI-1, a small molecule inhibitor of the eIF4E/eIF4G interaction that is under investigation as a novel anti-cancer drug, has a dual activity; it disrupts the eIF4E/eIF4G interaction and stabilizes the binding of 4E-BP1 to eIF4E. Here, we report the complete backbone NMR resonance assignment of an unliganded 4E-BP1 fragment (4E-BP144–87). We also report the near complete backbone assignment of the same fragment in complex to eIF4E/m7GTP (excluding the assignment of the last C-terminus residue, D87). The chemical shift data constitute a prerequisite to understanding the mechanism of action of translation initiation inhibitors, including 4EGI-1, that modulate the eIF4E/4E-BP1 interaction.
      PubDate: 2017-10-01
      DOI: 10.1007/s12104-017-9744-9
      Issue No: Vol. 11, No. 2 (2017)
  • Backbone NMR assignments of tryparedoxin, the central protein in the
           hydroperoxide detoxification cascade of African trypanosomes, in the
           oxidized and reduced form
    • Authors: Annika Wagner; Erika Diehl; R. Luise Krauth-Siegel; Ute A. Hellmich
      Pages: 193 - 196
      Abstract: Abstract Tryparedoxin (Tpx) is a pivotal protein in the redox-metabolism of trypanosomatid parasites. Tpx has previously been identified as a potential target for drug development in the fight against human African sleeping sickness caused by Trypanosoma brucei. Tpx belongs to the thioredoxin superfamily and acts as an oxidoreductase in the parasite’s cytoplasm. It contains a WCPPC active site motif, which enables the protein to undergo thiol-disulfide exchange. To promote future protein-drug interaction analyses, we report the 1H, 13C and 15N backbone chemical shift assignments for both the oxidized and reduced states of Tpx. The redox state of the protein has a significant impact on the chemical shifts of the residues at the active site of the protein, especially on the two redox active site cysteines. The NMR assignments presented here will be a prerequisite for investigating drug binding to Tpx in molecular detail and to drive further drug optimization.
      PubDate: 2017-10-01
      DOI: 10.1007/s12104-017-9746-7
      Issue No: Vol. 11, No. 2 (2017)
  • 1 H, 13 C and 15 N NMR assignments of a bacterial immunoglobulin-like
           domain (group 2) of a protein of a bacterium Paenarthrobacter aurescens
    • Authors: Asmita D. Pawar; Deepshikha Verma; Rajeev Raman; Yogendra Sharma; Kandala V. R. Chary
      Pages: 203 - 206
      Abstract: Abstract The bacterial immunoglobulin-like (Big) domain is one of the prevalent domain types, which facilitates cell–cell adhesion by assembling into multi-domain architectures. We selected a four Big_2 domain protein (named ‘Arig’) from a Gram positive, Paenarthrobacter aurescens TC1 (known earlier as Arthrobacter aurescens TC1). In an attempt to characterize structural and ligand-binding features of individual Big_2 domains, we have cloned, overexpressed, isolated and purified the second Big_2 domain of Arig along with a few of its adjacent Big_2 domain residues (residue 143 to 269) referred to as ‘Arig2’. The 13C/15N-doubly-labeled His-tagged Arig2 (133 residues long) showed an ordered conformation as revealed by the well dispersed 2D [15N-1H]-HSQC spectrum. Subsequently, a suite of heteronuclear 3D NMR experiments has enabled almost complete 1H, 13C and 15N NMR resonance assignments of Arig2.
      PubDate: 2017-10-01
      DOI: 10.1007/s12104-017-9748-5
      Issue No: Vol. 11, No. 2 (2017)
  • 1 H, 13 C and 15 N NMR chemical shift assignments of A. thaliana RCD1 RST
    • Authors: Helena Tossavainen; Maarit Hellman; Julia P. Vainonen; Jaakko Kangasjärvi; Perttu Permi
      Pages: 207 - 210
      Abstract: Abstract The A. thaliana RCD1 (radical-induced cell death1) protein is a cellular signaling hub protein which interacts with numerous plant transcription factors from different families. It consists of three conserved domains and intervening unstructured regions, the C-terminal RST domain being responsible for the interactions with the transcription factors. It has been shown that many partner proteins interact with RCD1 RST via their intrinsically disordered regions, and that the domain is able to house partners with divergent folds. We aim to structurally characterize the RCD1 RST domain and its complexes [complex with DREB2A]. Here we report the 1H, 15N and 13C chemical shift assignments of the backbone and sidechain atoms for RCD1 (468–589) containing the RST (510–567) domain.
      PubDate: 2017-10-01
      DOI: 10.1007/s12104-017-9749-4
      Issue No: Vol. 11, No. 2 (2017)
  • Backbone and side-chain assignments for a novel CBM69 starch binding
           domain AmyP-SBD
    • Authors: Xinxin Li; Jigang Yu; Jiahai Zhang; Hongbin Sun; Xuecheng Zhang
      Pages: 235 - 237
      Abstract: Abstract Starch binding domains (SBDs) are important for the functions of glycoside hydrolysis enzymes such as α-amylases, they have great application potential in biotechnology and industries. AmyP is a newly identified α-amylase belonging to a new subfamily 37 of glycoside hydrolysis enzyme family 13. AmyP shows preferential degradation to soluble starch, in which its C-terminal starch binding domain, AmyP-SBD, plays an important role. AmyP-SBD shares very low sequence similarity with other biochemically characterized SBDs and was assigned to a new carbohydrate binding module family CBM69. Intriguingly, AmyP-SBD is unfolded in free form, and substrate analogue β-cyclodextrin may induce it to fold into a relatively rigid state. Structure determination for AmyP-SBD will be helpful for understanding its unique properties. Here, we report the backbone and side-chain 1H, 13C and 15N resonance assignments of folded AmyP-SBD, as a basis for structure determination and further studies.
      PubDate: 2017-10-01
      DOI: 10.1007/s12104-017-9755-6
      Issue No: Vol. 11, No. 2 (2017)
  • 1 H, 15 N, 13 C backbone resonance assignments of human phosphoglycerate
           kinase in a transition state analogue complex with ADP, 3-phosphoglycerate
           and magnesium trifluoride
    • Authors: Zhalgas Serimbetov; Nicola J. Baxter; Matthew J. Cliff; Jonathan P. Waltho
      Abstract: Abstract Human phosphoglycerate kinase (PGK) is an energy generating glycolytic enzyme that catalyses the transfer of a phosphoryl group from 1,3-bisphosphoglycerate (BPG) to ADP producing 3-phosphoglycerate (3PG) and ATP. PGK is composed of two α/β Rossmann-fold domains linked by a central α-helix and the active site is located in the cleft formed between the N-domain which binds BPG or 3PG, and the C-domain which binds the nucleotides ADP or ATP. Domain closure is required to bring the two substrates into close proximity for phosphoryl transfer to occur, however previous structural studies involving a range of native substrates and substrate analogues only yielded open or partly closed PGK complexes. X-ray crystallography using magnesium trifluoride (MgF3 −) as a isoelectronic and near-isosteric mimic of the transferring phosphoryl group (PO3 −), together with 3PG and ADP has been successful in trapping human PGK in a fully closed transition state analogue (TSA) complex. In this work we report the 1H, 15N and 13C backbone resonance assignments of human PGK in the solution conformation of the fully closed PGK:3PG:MgF3:ADP TSA complex. Assignments were obtained by heteronuclear multidimensional NMR spectroscopy. In total, 97% of all backbone resonances were assigned in the complex, with 385 out of a possible 399 residues assigned in the 1H–15N TROSY spectrum. Prediction of solution secondary structure from a chemical shift analysis using the TALOS-N webserver is in good agreement with the published X-ray crystal structure of this complex.
      PubDate: 2017-09-02
      DOI: 10.1007/s12104-017-9758-3
  • NMR resonance assignments of the EVH1 domain of neurofibromin’s
           recruitment factor Spred1
    • Authors: Sebastian Führer; Linda Ahammer; Angela Ausserbichler; Klaus Scheffzek; Theresia Dunzendorfer-Matt; Martin Tollinger
      Abstract: Abstract Neurofibromin and Sprouty-related EVH1 domain-containing protein 1 (Spred1) both act as negative regulators of the mitogen-activated protein kinase pathway and are associated with the rare diseases Neurofibromatosis type 1 and Legius syndrome, respectively. Spred1 recruits the major GTPase activating protein (GAP) neurofibromin from the cytosol to the membrane in order to inactivate the small G protein Ras. These functions are dependent on the N-terminal EVH1 domain and the C-terminal Sprouty domain of Spred1 whereas the former specifically recognizes the GAP related domain of neurofibromin and the latter is responsible for membrane targeting. Within the GAP domain, Spred1 binding depends on the GAPex portion which is dispensable for Ras inactivation. In a first step towards the characterization of the Neurofibromin Spred1 interface in solution we assigned backbone and side chain 1H, 13C, and 15N chemical shifts of the Spred1 derived EVH1 domain. Our chemical shift data analysis indicate seven consecutive β-strands followed by a C-terminal α-helix which is in agreement with the previously reported crystal structure of Spred1(EVH1). Our data provide a framework for further analysis of the function of patient-derived mutations associated with rare diseases.
      PubDate: 2017-08-22
      DOI: 10.1007/s12104-017-9768-1
  • Chemical shift assignments of polyketide cyclase_like protein CGL2373 from
           Corynebacterium glutamicum
    • Authors: Chunjie Liang; Rui Hu; Theresa A. Ramelot; Michael A. Kennedy; Xuegang Li; Yunhuang Yang; Jiang Zhu; Maili Liu
      Abstract: Abstract Protein CGL2373 from Corynebacterium glutamicum, which is 155 amino acids long and 17.7 kDa, is a member of the polyketide_cyc2 family. As a potential polyketide cyclase, it may play an important role in the biosynthesis of aromatic polyketides that are the source of many bioactive molecules. Here we report the complete 1H, 13C and 15N chemical shift assignments of CGL2373, which lays a foundation for further structural and functional research.
      PubDate: 2017-08-20
      DOI: 10.1007/s12104-017-9765-4
  • Backbone resonance assignments of complexes of human voltage-dependent
           sodium channel Na V 1.2 IQ motif peptide bound to apo calmodulin and to
           the C-domain fragment of apo calmodulin
    • Authors: Ryan Mahling; Adina M. Kilpatrick; Madeline A. Shea
      Abstract: Abstract Human voltage-gated sodium channel NaV1.2 has a single pore-forming α-subunit and two transmembrane β-subunits. Expressed primarily in the brain, NaV1.2 is critical for initiation and propagation of action potentials. Milliseconds after the pore opens, sodium influx is terminated by inactivation processes mediated by regulatory proteins including calmodulin (CaM). Both calcium-free (apo) CaM and calcium-saturated CaM bind tightly to an IQ motif in the C-terminal tail of the α-subunit. Our thermodynamic studies and solution structure (2KXW) of a C-domain fragment of apo 13C,15N- CaM (CaMC) bound to an unlabeled peptide with the sequence of rat NaV1.2 IQ motif showed that apo CaMC (a) was necessary and sufficient for binding, and (b) bound more favorably than calcium-saturated CaMC. However, we could not monitor the NaV1.2 residues directly, and no structure of full-length CaM (including the N-domain of CaM (CaMN)) was determined. To distinguish contributions of CaMN and CaMC, we used solution NMR spectroscopy to assign the backbone resonances of a complex containing a 13C,15N-labeled peptide with the sequence of human NaV1.2 IQ motif (NaV1.2IQp) bound to apo 13C,15N-CaM or apo 13C,15N-CaMC. Comparing the assignments of apo CaM in complex with NaV1.2IQp to those of free apo CaM showed that residues within CaMC were significantly perturbed, while residues within CaMN were essentially unchanged. The chemical shifts of residues in NaV1.2IQp and in the C-domain of CaM were nearly identical regardless of whether CaMN was covalently linked to CaMC. This suggests that CaMN does not influence apo CaM binding to NaV1.2IQp.
      PubDate: 2017-08-19
      DOI: 10.1007/s12104-017-9767-2
  • Backbone and side-chain resonance assignments of (Ca 2+ ) 4 –calmodulin
           bound to beta calcineurin A CaMBD peptide
    • Authors: C. Andrew Fowler; Maria F. Núñez Hernandez; Susan E. O’Donnell; Liping Yu; Madeline A. Shea
      Abstract: Abstract Calcineurin (CaN) is a heterodimeric and highly conserved serine/threonine phosphatase (PP2B) that plays a critical role in coupling calcium signals to physiological processes including embryonic cardiac development, NF-AT-regulated gene expression in immune responses, and apoptosis. The catalytic subunit (CaNA) has three isoforms (α, β, and γ,) in humans and seven isoforms in Paramecium. In all eukaryotes, the EF-hand protein calmodulin (CaM) regulates CaN activity in a calcium-dependent manner. The N- and C-domains of CaM (CaMN and CaMC) recognize a CaM-binding domain (CaMBD) within an intrinsically disordered region of CaNA that precedes the auto-inhibitory domain (AID) of CaNA. Here we present nearly complete 1H, 13C, and 15N resonance assignments of (Ca2+)4–CaM bound to a peptide containing the CaMBD sequence in the beta isoform of CaNA (βCaNA–CaMBDp). Its secondary structure elements predicted from the assigned chemical shifts were in good agreement with those observed in the high-resolution structures of (Ca2+)4–CaM bound to CaMBDs of multiple enzymes. Based on the reported literature, the CaMBD of the α isoform of CaNA can bind to CaM in two opposing orientations which may influence the regulatory function of CaM. Because a high resolution structure of (Ca2+)4–CaM bound to βCaNA–CaMBDp has not been reported, our studies serve as a starting point for determining the solution structure of this complex. This will demonstrate the preferred orientation of (Ca2+)4–CaM on the CaMBD as well as the orientations of CaMN and CaMC relative to each other and to the AID of βCaNA.
      PubDate: 2017-08-16
      DOI: 10.1007/s12104-017-9762-7
  • Backbone resonance assignments for the SET domain of human
           methyltransferase NSD3 in complex with its cofactor
    • Authors: Yan Li; Hui Qi Ng; Anna Ngo; Shuang Liu; Yih Wan Tan; Perlyn Zekui Kwek; Alvin W. Hung; Joma Joy; Jeffrey Hill; Thomas H. Keller; CongBao Kang
      Abstract: Abstract NSD3 is a histone H3 methyltransferase that plays an important role in chromatin biology. A construct containing the methyltransferase domain encompassing residues Q1049-K1299 of human NSD3 was obtained and biochemical activity was demonstrated using histone as a substrate. Here we report the backbone HN, N, Cα, C′, and side chain Cβ assignments of the construct in complex with S-adenosyl-l-methionine (SAM). Based on these assignments, secondary structures of NSD3/SAM complex in solution were determined.
      PubDate: 2017-08-14
      DOI: 10.1007/s12104-017-9753-8
  • Backbone and side chain assignments of the second RNA-binding domain of
           Musashi-1 in its free form and in complex with 5-mer RNA
    • Authors: Ryo Iwaoka; Takashi Nagata; Kengo Tsuda; Takao Imai; Hideyuki Okano; Naohiro Kobayashi; Masato Katahira
      Abstract: Abstract Musashi1 (Msi1) is an RNA-binding protein that is involved in cell fate determination. Here, we report the 1H, 15N, and 13C resonance assignments of Msi1 second RNA-binding domain in free form and in complex with RNA. The assignments can be utilized for NMR structure and dynamics analyses of the Msi1:RNA complex, and moreover, for chemical shift perturbation analyses to evaluate the binding of potential small molecule inhibitors against Msi1:RNA interaction.
      PubDate: 2017-08-14
      DOI: 10.1007/s12104-017-9760-9
  • NMR backbone resonance assignment of New Delhi metallo-beta-lactamase
    • Authors: Chendie Yao; Qiong Wu; Guohua Xu; Conggang Li
      Abstract: Abstract The emerging of the New Delhi metallo-beta-lactamase (NDM-1) has become one of the greatest threats to the clinical treatment. Although the structure of NDM-1 has been determined by X-ray crystallography, the molecular mechanism and process of catalysis reaction remain elusive. NMR spectroscopy plays a unique role in the characterization of conformational dynamics. Here we report the backbone 1H, 15N and 13C chemical shift assignments of NDM-1 by heteronuclear multidimensional NMR spectroscopy as well as its secondary structure in solution as predicted by TALOS+.
      PubDate: 2017-08-14
      DOI: 10.1007/s12104-017-9756-5
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