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CHEMISTRY (532 journals)                  1 2 3 4 5 6 | Last

2D Materials     Hybrid Journal   (Followers: 1)
Accreditation and Quality Assurance: Journal for Quality, Comparability and Reliability in Chemical Measurement     Hybrid Journal   (Followers: 31)
ACS Catalysis     Full-text available via subscription   (Followers: 23)
ACS Chemical Neuroscience     Full-text available via subscription   (Followers: 13)
ACS Combinatorial Science     Full-text available via subscription   (Followers: 8)
ACS Macro Letters     Full-text available via subscription   (Followers: 17)
ACS Medicinal Chemistry Letters     Full-text available via subscription   (Followers: 25)
ACS Nano     Full-text available via subscription   (Followers: 250)
ACS Photonics     Full-text available via subscription   (Followers: 2)
ACS Synthetic Biology     Full-text available via subscription   (Followers: 8)
Acta Chemica Iasi     Open Access  
Acta Chimica Slovaca     Open Access   (Followers: 5)
Acta Chromatographica     Full-text available via subscription   (Followers: 10)
Acta Facultatis Medicae Naissensis     Open Access   (Followers: 1)
Acta Metallurgica Sinica (English Letters)     Hybrid Journal   (Followers: 4)
adhäsion KLEBEN & DICHTEN     Hybrid Journal   (Followers: 2)
Adhesion Adhesives & Sealants     Hybrid Journal   (Followers: 4)
Adsorption Science & Technology     Full-text available via subscription   (Followers: 8)
Advanced Functional Materials     Hybrid Journal   (Followers: 32)
Advances in Chemical Engineering and Science     Open Access   (Followers: 21)
Advances in Chemical Science     Open Access   (Followers: 8)
Advances in Colloid and Interface Science     Full-text available via subscription   (Followers: 13)
Advances in Drug Research     Full-text available via subscription   (Followers: 17)
Advances in Fluorine Science     Full-text available via subscription   (Followers: 7)
Advances in Fuel Cells     Full-text available via subscription   (Followers: 12)
Advances in Heterocyclic Chemistry     Full-text available via subscription   (Followers: 8)
Advances in Materials Physics and Chemistry     Open Access   (Followers: 13)
Advances in Nanoparticles     Open Access   (Followers: 11)
Advances in Organometallic Chemistry     Full-text available via subscription   (Followers: 8)
Advances in Polymer Science     Hybrid Journal   (Followers: 38)
Advances in Protein Chemistry     Full-text available via subscription   (Followers: 6)
Advances in Protein Chemistry and Structural Biology     Full-text available via subscription   (Followers: 10)
Advances in Quantum Chemistry     Full-text available via subscription   (Followers: 4)
African Journal of Chemical Education     Open Access   (Followers: 1)
African Journal of Pure and Applied Chemistry     Open Access   (Followers: 3)
Afrique Science : Revue Internationale des Sciences et Technologie     Open Access  
Agrokémia és Talajtan     Full-text available via subscription   (Followers: 2)
Alchemy     Open Access   (Followers: 2)
Alkaloids: Chemical and Biological Perspectives     Full-text available via subscription   (Followers: 4)
AMB Express     Open Access   (Followers: 1)
American Journal of Applied Sciences     Open Access   (Followers: 28)
American Journal of Biochemistry and Biotechnology     Open Access   (Followers: 150)
American Journal of Biochemistry and Molecular Biology     Open Access   (Followers: 11)
American Journal of Chemistry     Open Access   (Followers: 17)
American Journal of Plant Physiology     Open Access   (Followers: 9)
American Mineralogist     Full-text available via subscription   (Followers: 2)
Analyst     Full-text available via subscription   (Followers: 34)
Angewandte Chemie     Hybrid Journal   (Followers: 15)
Angewandte Chemie International Edition     Hybrid Journal   (Followers: 201)
Annales UMCS, Chemia     Open Access   (Followers: 2)
Annual Reports in Computational Chemistry     Full-text available via subscription   (Followers: 1)
Annual Reports Section A (Inorganic Chemistry)     Full-text available via subscription   (Followers: 2)
Annual Reports Section B (Organic Chemistry)     Full-text available via subscription   (Followers: 4)
Annual Review of Chemical and Biomolecular Engineering     Full-text available via subscription   (Followers: 10)
Annual Review of Food Science and Technology     Full-text available via subscription   (Followers: 12)
Anti-Infective Agents     Hybrid Journal   (Followers: 1)
Applied Organometallic Chemistry     Hybrid Journal   (Followers: 4)
Applied Spectroscopy     Full-text available via subscription   (Followers: 12)
Applied Surface Science     Hybrid Journal   (Followers: 14)
Arabian Journal of Chemistry     Full-text available via subscription   (Followers: 6)
ARKIVOC     Open Access   (Followers: 1)
Asian Journal of Biochemistry     Open Access   (Followers: 1)
Australian Journal of Chemistry     Hybrid Journal   (Followers: 4)
Autophagy     Full-text available via subscription   (Followers: 1)
Avances en Quimica     Open Access   (Followers: 1)
Biochemical Pharmacology     Hybrid Journal   (Followers: 6)
Biochemistry     Full-text available via subscription   (Followers: 187)
Biochemistry Insights     Open Access   (Followers: 4)
Biochemistry Research International     Open Access   (Followers: 4)
BioChip Journal     Hybrid Journal   (Followers: 1)
Bioinorganic Chemistry and Applications     Open Access   (Followers: 4)
Biointerface Research in Applied Chemistry     Open Access   (Followers: 1)
Biointerphases     Open Access  
Biomacromolecules     Full-text available via subscription   (Followers: 17)
Biomass Conversion and Biorefinery     Partially Free   (Followers: 5)
Biomedical Chromatography     Hybrid Journal   (Followers: 7)
Biomolecular NMR Assignments     Hybrid Journal   (Followers: 2)
BioNanoScience     Partially Free   (Followers: 4)
Bioorganic & Medicinal Chemistry     Hybrid Journal   (Followers: 30)
Bioorganic & Medicinal Chemistry Letters     Hybrid Journal   (Followers: 24)
Bioorganic Chemistry     Hybrid Journal   (Followers: 5)
Biopolymers     Hybrid Journal   (Followers: 13)
Biosensors     Open Access   (Followers: 3)
Biotechnic and Histochemistry     Hybrid Journal   (Followers: 1)
Boletin de la Sociedad Chilena de Quimica     Open Access  
Bulletin of the Chemical Society of Ethiopia     Open Access   (Followers: 1)
Bulletin of the Chemical Society of Japan     Full-text available via subscription   (Followers: 12)
Canadian Association of Radiologists Journal     Full-text available via subscription   (Followers: 3)
Canadian Journal of Chemistry     Full-text available via subscription   (Followers: 6)
Canadian Mineralogist     Full-text available via subscription   (Followers: 1)
Carbohydrate Research     Hybrid Journal   (Followers: 10)
Carbon     Hybrid Journal   (Followers: 37)
Catalysis for Sustainable Energy     Open Access   (Followers: 2)
Catalysis Reviews: Science and Engineering     Hybrid Journal   (Followers: 4)
Catalysis Science and Technology     Free   (Followers: 4)
Catalysis Surveys from Asia     Hybrid Journal   (Followers: 4)
Catalysts     Open Access   (Followers: 6)
Cellulose     Hybrid Journal   (Followers: 4)
Central European Journal of Chemistry     Hybrid Journal   (Followers: 5)
Cereal Chemistry     Full-text available via subscription   (Followers: 3)

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Journal Cover Biomolecular NMR Assignments
   Journal TOC RSS feeds Export to Zotero [4 followers]  Follow    
   Hybrid Journal Hybrid journal (It can contain Open Access articles)
     ISSN (Print) 1874-270X - ISSN (Online) 1874-2718
     Published by Springer-Verlag Homepage  [2210 journals]   [SJR: 0.402]   [H-I: 7]
  • Backbone and side chain NMR assignments for the ribosome assembly factor
           Nop6 from Saccharomyces
    • Abstract: Abstract The Saccharomyces cerevisiae Nop6 protein is involved in the maturation of the small ribosomal subunit. It contains a central RNA binding domain and a predicted C-terminal coiled-coil domain. Here we report the almost complete (>90 %) 1H,13C,15N backbone and side chain NMR assignment of a 15 kDa Nop6 construct comprising the RNA binding and coiled-coil domains.
      PubDate: 2014-10-01
  • Erratum to: Backbone 1H, 13C and 15N assignments of YibK and a variant
           containing a unique cysteine residue at C-terminus in 8 M urea-denatured
    • PubDate: 2014-10-01
  • Resonance assignments of the microtubule-binding domain of the        class="a-plus-plus">C. elegans spindle and
           kinetochore-associated protein 1
    • Abstract: Abstract During mitosis, kinetochores coordinate the attachment of centromeric DNA to the dynamic plus ends of microtubules, which is hypothesized to pull sister chromatids toward opposing poles of the mitotic spindle. The outer kinetochore Ndc80 complex acts synergistically with the Ska (spindle and kinetochore-associated) complex to harness the energy of depolymerizing microtubules and power chromosome movement. The Ska complex is a hexamer consisting of two copies of the proteins Ska1, Ska2 and Ska3, respectively. The C-terminal domain of the spindle and kinetochore-associated protein 1 (Ska1) is the microtubule-binding domain of the Ska complex. We solved the solution structure of the C. elegans microtubule-binding domain (MTBD) of the protein Ska1 using NMR spectroscopy. Here, we report the resonance assignments of the MTBD of C. elegans Ska1.
      PubDate: 2014-10-01
  • NMR assignments of a hypothetical pseudo-knotted protein HP0242 from
           Helicobacter pylori
    • Abstract: Abstract Many knotted proteins have been discovered recently, but the folding process of which remains elusive. HP0242 is a hypothetical protein from Helicobacter pylori, which is a model system for studying the folding pathway of a knotted protein. In this study, we report the 1H, 13C, and 15N chemical shift assignments of HP0242. The results will enable us to further investigate HP0242 by NMR experiments.
      PubDate: 2014-10-01
  • Backbone 1H,        class="a-plus-plus">15N,        class="a-plus-plus">13C and side chain        class="a-plus-plus">13Cβ NMR chemical shift
           assignment of murine interleukin-10
    • Abstract: Abstract Almost complete assignment of backbone 1H, 13C, 15N and side chain 13Cβ resonances for the immune-regulatory cytokine IL-10 is reported. The protein was overexpressed in Escherichia coli and was refolded from inclusion bodies. The point mutation C149Y was introduced to suppress incorrect disulfide bond formation and to improve protein refolding.
      PubDate: 2014-10-01
  • Yet another polymorph of α-synuclein: solid-state sequential
    • Abstract: Abstract Parkinson’s disease is a neurological human proteinopathy, which is caused by the accumulation of protein aggregates of high molecular mass. α-Synuclein is a major component of these fibrillar, β-sheet rich, insoluble assemblies and is deposited in the form of amyloids. Structural characterization of amyloids is possible by solid-state NMR, although no atomic-resolution structure is available as of today. α-Synuclein, as many other pathology-related fibril-forming proteins, can form a number of different polymorphs that are sometimes tricky to obtain in pure form. Here, we describe the chemical shifts and secondary structure analysis of a polymorph that also adopts mainly β-sheet conformation, with a fibrillar core ranging from residues 38 to 94. In addition, residues 15–20 from the N-terminus found to be part of a rigid ordered β-sheet. The chemical shifts differ substantially from the polymorph we previously assigned.
      PubDate: 2014-10-01
  • 1H,        class="a-plus-plus">13C and        class="a-plus-plus">15N backbone and side-chain
           resonance assignments of a family 36 carbohydrate binding module of
           xylanase from Paenibacillus
    • Abstract: Abstract Paenibacillus campinasensis BL11 isolated from black liquor secretes multiple glycoside hydrolases (GHs) against all kinds of polysaccharides. GH consists of a catalytic module and non-catalytic carbohydrate-binding modules (CBMs), in which CBMs append to the catalytic module, mediating specific interactions with insoluble carbohydrates to promote the hydrolysis efficiency of the cognate enzyme. Endo-β-1,4-xylanase (XylX) is one of the GHs reveals high enzymatic activity in a wide range of pH and thermal endurance, suitable for bioconversion and bio-refinement applications. In this work, we report the resonance assignments of a family 36 CBM (characterized as CBM36) derived from XylX. Our investigations will facilitate molecular structure determination and molecular dynamics analysis of CBMs.
      PubDate: 2014-10-01
  • 1H,        class="a-plus-plus">15N, and        class="a-plus-plus">13C backbone resonance
           assignments for the        class="a-plus-plus">yersinia protein tyrosine
           phosphatase YopH
    • Abstract: Abstract YopH is a protein tyrosine phosphatase that functions as a required virulence factor in Yersinia. Here we report the backbone resonance assignments for a point mutant of the C-terminal catalytic domain of YopH.
      PubDate: 2014-10-01
  • Backbone and side-chain        class="a-plus-plus">1H,        class="a-plus-plus">13C and        class="a-plus-plus">15N resonance assignments of
           the OB domain of the single stranded DNA binding protein from        class="a-plus-plus">Sulfolobus solfataricus and
           chemical shift mapping of the DNA-binding interface
    • Abstract: Abstract Single stranded DNA binding proteins (SSBs) are present in all known cellular organisms and are critical for DNA replication, recombination and repair. The SSB from the hyperthermophilic crenarchaeote Sulfolobus solfataricus (SsoSSB) has an unusual domain structure with a single DNA-binding oligonucleotide binding (OB) fold coupled to a flexible C-terminal tail. This ‘simple’ domain organisation differs significantly from other known SSBs, such as human replication protein A (RPA). However, it is conserved in another important human SSB, hSSB1, which we have recently discovered and shown to be essential in the DNA damage response. In this study we report the solution-state backbone and side-chain chemical shift assignments of the OB domain of SsoSSB. In addition, using the recently determined crystal structure, we have utilized NMR to reveal the DNA-binding interface of SsoSSB. These data will allow us to elucidate the structural basis of DNA-binding and shed light onto the molecular mechanism by which these ‘simple’ SSBs interact with single-stranded DNA.
      PubDate: 2014-10-01
  • Backbone resonance assignments of the 42 kDa enzyme arginine kinase
           in the transition state analogue form
    • Abstract: Abstract Nearly complete backbone resonance assignments for the 357 residue, 42 kDa enzyme arginine kinase in a transition state analogue (TSA) complex are presented. The TSA is a quaternary complex of arginine kinase, MgADP, arginine, and nitrate. About 93 % (320 of 344) of the non-proline backbone amides were assigned using an enzyme enriched with 2H, 13C, and 15N in combination with three enzyme samples prepared with a single 15N-labeled amino acid (K, L, and R). The amide assignments will provide the foundation for investigating the dynamics of arginine kinase when in a TSA complex.
      PubDate: 2014-10-01
  • Backbone resonance assignments of human cytosolic dNT-1 nucleotidase
    • Abstract: Abstract Cytosolic dNT-1 nucleotidase plays a key role in the homeostasis of pyrimidine deoxyribonucleotides in mammalian cells. The enzyme is responsible for the dephosphorylation of physiological substrates as well as nucleoside analogues that are used in antiviral and anticancer therapies, therefore selective inhibition of the dNT-1 nucleotidase activity may lead to an increase in efficacy of this type of therapeutic compounds. Here, we report the backbone 1H, 13C and 15N assignments for the 47 kDa dNT-1 dimer, which will be used for structural characterisation of dNT-1 complexes with small molecule inhibitors obtained through modification of pyrimidine nucleotide scaffolds or optimisation of successful binders obtained from the screening of fragment libraries.
      PubDate: 2014-10-01
  • Chemical shift assignments of the C-terminal Eps15 homology domain-3 EH
    • Abstract: Abstract The C-terminal Eps15 homology (EH) domain 3 (EHD3) belongs to a eukaryotic family of endocytic regulatory proteins and is involved in the recycling of various receptors from the early endosome to the endocytic recycling compartment or in retrograde transport from the endosomes to the Golgi. EH domains are highly conserved in the EHD family and function as protein-protein interaction units that bind to Asn-Pro-Phe (NPF) motif-containing proteins. The EH domain of EHD1 was the first C-terminal EH domain from the EHD family to be solved by NMR. The differences observed between this domain and proteins with N-terminal EH domains helped describe a mechanism for the differential binding of NPF-containing proteins. Here, structural studies were expanded to include the EHD3 EH domain. While the EHD1 and EHD3 EH domains are highly homologous, they have different protein partners. A comparison of these structures will help determine the selectivity in protein binding between the EHD family members and lead to a better understanding of their unique roles in endocytic regulation.
      PubDate: 2014-10-01
  • Backbone and side-chain assignments of an effector membrane localization
           domain from Vibrio
    MARTX toxin
    • Abstract: Abstract 1H, 13C, and 15N chemical shift assignments are presented for the isolated four-helical bundle membrane localization domain from the domain of unknown function 5 (DUF5) effector (MLDVvDUF5) of the MARTX toxin from Vibrio vulnificus in its solution state. We have assigned 97 % of all backbone and side-chain carbon atoms, including 96 % of all backbone residues. Secondary chemical shift analysis using TALOS+ demonstrates four helices that align with those predicted by structure homology modeling using the MLDs of Pasteurella multocida toxin (PMT) and the clostridial TcdB and TcsL toxins as templates. Future studies will be towards solving the structure and determining the dynamics in the solution state.
      PubDate: 2014-10-01
  • 1H,        class="a-plus-plus">15N, and        class="a-plus-plus">13C chemical shift
           assignments of murine calcium-binding protein 4
    • Abstract: Abstract Calcium-binding protein 4 (CaBP4) regulates voltage-gated Ca2+ channels in retinal rod cells and specific mutations within CaBP4 are associated with congenital stationary night blindness type 2. We report complete NMR chemical shift assignments of the Ca2+-saturated form of CaBP4 with Ca2+ bound at EF1, EF3 and EF4 (BMRB no. 18877).
      PubDate: 2014-10-01
  • 1H,        class="a-plus-plus">13C, and        class="a-plus-plus">15N NMR assignments of a
           Drosophila Hedgehog
           autoprocessing domain
    • Abstract: Abstract The Hedgehog (Hh) signaling pathway plays important roles in embryonic growth and patterning in different organisms. Abnormal activity of the Hh signaling pathway has been associated to cancers, holoprosencephaly and autism spectrum disorders. The backbone and side chain resonance assignments of a Drosophila Hh autoprocessing domain have been determined based on triple-resonance experiments with the [13C, 15N]-labeled and [2H, 13C, 15N])-labeled proteins.
      PubDate: 2014-10-01
  • 13C,        class="a-plus-plus">15N and        class="a-plus-plus">1H backbone and side chain
    • Abstract: Abstract HdeA is a small chaperone found in the periplasm of several common pathogenic bacteria (Escherichia coli, Shigella flexneri and Brucella abortus) which are the leading causes of dysentery worldwide, especially in developing countries. Its job is to protect other periplasmic proteins from aggregating as the bacteria pass through the low pH environment of the human stomach on their way to infect the intestines. HdeA is an inactive folded dimer at neutral pH, but becomes a disordered active monomer at pH < 3. To initiate NMR characterization of HdeA at pH 6, 94 % of the backbone and 86 % of the side chain chemical shifts have been assigned. The loop linking helices B and C remains largely unassigned due to missing peaks in the 1H–15N HSQC and other spectra, most likely due to intermediate timescale chemical exchange. Many of the weakest intensity backbone peaks correspond to residues that surround this loop within the tertiary structure. Assignment experiments have therefore helped to provide preliminary clues about the region of the protein that may be most responsible for initiating unfolding as the pH drops, and constitute an important first step in improving our understanding of, and ultimately combatting, HdeA activity.
      PubDate: 2014-10-01
  • 1H,        class="a-plus-plus">13C and        class="a-plus-plus">15N backbone and side-chain
           resonance assignments of the N-terminal ubiquitin-binding domains of USP25
    • Abstract: Abstract Ubiquitin Specific Protease 25 (USP25), a member of the deubiquitinase family, is involved in several disease-related signal pathways including myogenesis, immunity and protein degradation. It specially catalyzes the hydrolysis of the K48-linked and K63-linked polyubiquitin chains. USP25 contains one ubiquitin-associated domain and two ubiquitin-interacting motifs (UIMs) in its N-terminal region, which interact with ubiquitin and play a role in substrate recognition. Besides, it has been shown that the catalysis activity of USP25 is either impaired by sumoylation or enhanced by ubiquitination within its UIM. To elucidate the structural basis of the cross-regulation of USP25 function by non-covalent binding and covalent modifications of ubiquitin and SUMO2/3, a systematic structural biology study of USP25 is required. Here, we report the 1H, 13C and 15N backbone and side-chain resonance assignments of the N-terminal ubiquitin binding domains (UBDs) of USP25 with BMRB accession number of 19111, which is the first step of the systematic structural biology study of the enzyme.
      PubDate: 2014-10-01
  • Solid-state NMR sequential assignments of the amyloid core of full-length
    • Abstract: Abstract Sup35p is a yeast prion and is responsible for the [PSI +] trait in Saccharomyces cerevisiae. With 685 amino acids, full-length soluble and fibrillar Sup35p are challenging targets for structural biology as they cannot be investigated by X-ray crystallography or NMR in solution. We present solid-state NMR studies of fibrils formed by the full-length Sup35 protein. We detect an ordered and rigid core of the protein that gives rise to narrow and strong peaks, while large parts of the protein show either static disorder or dynamics on time scales which interfere with dipolar polarization transfer or shorten the coherence lifetime. Thus, only a small subset of resonances is observed in 3D spectra. Here we describe in detail the sequential assignments of the 22 residues for which resonances are observed in 3D spectra: their chemical shifts mostly corresponding to β-sheet secondary structure. We suspect that these residues form the amyloid core of the fibril.
      PubDate: 2014-10-01
  • NMR assignments of PI3-SH3 domain aided by protonless NMR spectroscopy
    • Abstract: Abstract We report here the near complete assignments of native bovine PI3-SH3 domain, which has been a model system for protein folding, misfolding and amyloid fibril formation. The use of 13C-detected protonless NMR spectroscopy is instrumental in assigning the spin system of the proline residue at the C-terminus in addition to the missing resonances in proton-based NMR spectra due to rapid solvent exchange. It also helps assign the resonances of all three proline amine nitrogen nuclei, which are underrepresented in the database. Comparison of the backbone 13C resonances of PI3-SH3 in its native and amyloid fibril states shows that the aggregation of PI3-SH3 is accompanied by major conformational rearrangements.
      PubDate: 2014-10-01
  • Chemical shift assignments of a reduced N-terminal truncation mutant of
           the disulfide bond isomerase TrbB from plasmid F, TrbBΔ29
    • Abstract: Abstract TrbB from the conjugative plasmid F is a 181-residue disulfide bond isomerase that plays a role in the correct folding and maintenance of disulfide bonds within F plasmid encoded proteins in the bacterial periplasm. As a member of the thioredoxin-like superfamily, TrbB has a predicted thioredoxin-like fold that contains a C–X–X–C active site required for performing specific redox chemistries on protein substrates. Here we report the sequence-specific assignments of the reduced form of the N-terminally truncated TrbB construct, TrbBΔ29.
      PubDate: 2014-04-26
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