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  Subjects -> CHEMISTRY (Total: 766 journals)
    - ANALYTICAL CHEMISTRY (45 journals)
    - CHEMISTRY (531 journals)
    - CRYSTALLOGRAPHY (22 journals)
    - ELECTROCHEMISTRY (24 journals)
    - INORGANIC CHEMISTRY (40 journals)
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CHEMISTRY (531 journals)                  1 2 3 4 5 6 | Last

2D Materials     Hybrid Journal  
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: 7)
ACS Macro Letters     Full-text available via subscription   (Followers: 17)
ACS Medicinal Chemistry Letters     Full-text available via subscription   (Followers: 24)
ACS Nano     Full-text available via subscription   (Followers: 237)
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: 2)
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: 12)
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: 2)
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: 27)
American Journal of Biochemistry and Biotechnology     Open Access   (Followers: 142)
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: 35)
Angewandte Chemie     Hybrid Journal   (Followers: 15)
Angewandte Chemie International Edition     Hybrid Journal   (Followers: 189)
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  
Avances en Quimica     Open Access   (Followers: 1)
Biochemical Pharmacology     Hybrid Journal   (Followers: 6)
Biochemistry     Full-text available via subscription   (Followers: 173)
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: 12)
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: 36)
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)

        1 2 3 4 5 6 | Last

Journal Cover Biomolecular NMR Assignments
   [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]
  • 1H,        class="a-plus-plus">15N and        class="a-plus-plus">13C chemical shift
           assignments of the homeodomain of Hoxc9 in complex with the cell cycle
           regulator Geminin
    • Abstract: Abstract Homeodomain-containing transcription factors including Hox proteins play fundamental roles in the regulation of different cellular and developmental processes. These proteins all contain a homeodomain, which is a 60-amino acid DNA binding domain encoded by a 180-base pair DNA sequence. Homeodomains also serve as protein interaction targets to regulate the functions of these transcription factors or other proteins. The cell cycle regulator Geminin interacts with Hox homeodomains to inhibit the transcription activities of Hox proteins and enrolls Hox proteins in the cell proliferation process. Here we report complete chemical shift assignments of the homeodomain of Hoxc9 (Hoxc9-HD) in complex with the homeodomain binding region of Geminin (Gem-HBR), which were determined by triple resonance NMR experiments. These resonance assignments provide a basis for the structure determination of the Hoxc9-HD/Gem-HBR complex and for the further study of homeodomains in complex with other regulatory protein partners (BMRB deposits with accession number 17407).
      PubDate: 2014-08-05
       
  • 1H,        class="a-plus-plus">13C and        class="a-plus-plus">15N chemical shift
           assignments of the NDH-1 complex subunit CupS
    • Abstract: Abstract The cyanobacterial NDH-1 complex is involved in respiratory as well as in cyclic electron transfer around photosystem I. Here, we report both backbone and side chain chemical shift assignments of CupS, a small subunit of the multisubunit membrane protein complex NDH-1 from Thermosynechococcus elongatus. The construct contains 159 amino acids including a Strep-tag and two additional amino acids.
      PubDate: 2014-07-20
       
  • NMR resonance assignments of the archaeal ribosomal protein L7Ae in the
           apo form and bound to a 25 nt RNA
    • Abstract: Abstract The archaeal protein L7Ae forms part of a protein complex in the ribosome that specifically recognizes and binds to kink-turn RNA. In this complex, L7Ae directly interacts with the oligonucleotide and creates a functional arrangement for site-specific 2′-O-methylation. We report the solution NMR backbone assignment of Methanocaldococcus jannaschii L7Ae (117 residues, 12.7 kDa) in the ligand-free state and when bound to a 25 nucleotide C/D box kink-turn mimic RNA.
      PubDate: 2014-07-17
       
  • Sequence-specific backbone        class="a-plus-plus">1H,        class="a-plus-plus">13C, and        class="a-plus-plus">15N resonance assignments of
           human ribonuclease 4
    • Abstract: Abstract Human ribonuclease 4 (RNase 4) is the most evolutionarily conserved member of the 8 canonical human pancreatic-like RNases, showing more than 90 % identity with bovine and porcine homologues. The enzyme displays ribonucleolytic activity with a strong preference for uracil-containing RNA substrates, a feature only shared with human eosinophil derived-neurotoxin (EDN, or RNase 2) and eosinophil cationic protein (ECP, or RNase 3). It is also the shortest member of the human family, with a significantly truncated C-terminal tail. Its unique active-site pocket and high degree of conservation among vertebrates suggest that the enzyme plays a crucial biological function. Here, we report on the 1H, 13C and 15N backbone resonance assignments of RNase 4, providing means to characterize its molecular function at the atomic level by NMR.
      PubDate: 2014-07-17
       
  • 1H,        class="a-plus-plus">15N and        class="a-plus-plus">13C resonance assignments and
           secondary structure prediction of Q4D059, a conserved and
           kinetoplastid-specific hypothetical protein from        class="a-plus-plus">Trypanosoma cruzi
    • Abstract: Abstract Trypanosoma cruzi is a human parasite that causes Chagas disease, an illness affecting millions of people and without an efficient treatment available. Sequencing the pathogen genome has revealed that near half of protein-coding genes correspond to hypothetical proteins of unknown function, increasing the possibilities for novel target discovery. Q4D059 is a putative essential hypothetical protein from T. cruzi and it is specific and conserved among the trypanosomatid genomes. Here, we report the sequential backbone and side chain resonance assignments and secondary structure analysis of Q4D059, as first step for protein structure determination, function elucidation and drug screening.
      PubDate: 2014-07-15
       
  • NMR assignment of the amylase-binding protein A from        class="a-plus-plus">Streptococcus parasanguinis
    • Abstract: Abstract Streptococcus parasanguinis is a primary colonizer of tooth surfaces in the oral cavity. Amylase-binding protein A (AbpA) from S. parasanguinis is responsible for the recruitment of salivary amylase to bacterial surface, which plays an important role in the development of oral biofilms. Here, we describe the essentially complete NMR assignments for AbpA.
      PubDate: 2014-07-14
       
  • 1H,        class="a-plus-plus">13C, and        class="a-plus-plus">15N backbone and sidechain
           chemical shift assignments for the HEAT2 domain of human eIF4GI
    • Abstract: Abstract The translation initiation factor eIF4G is required for the translation of many eukaryotic messenger RNAs. Its interaction with the ATP-dependent RNA helicase eIF4A plays an important role in the regulation of translation initiation. eIF4G in humans and other higher eukaryotes contains three HEAT domains, of which HEAT1 and HEAT2 contain binding sites for eIF4A. Here we report the near complete NMR resonance assignment of the 192-residue HEAT2 domain of the human translation initiation factor eIF4GI. The chemical shift data constitute the basis for NMR structural studies aimed at expanding understanding of the role of interactions between the initiation factor eIF4A and eIF4G in translation initiation.
      PubDate: 2014-06-15
       
  • 1H,        class="a-plus-plus">13C and        class="a-plus-plus">15N resonance assignment of
           the mature form of monothiol glutaredoxin 1 from the pathogen        class="a-plus-plus">Trypanosoma brucei
    • Abstract: Abstract Glutaredoxins (Grx) are small proteins, conserved throughout all the kingdoms of life, which are engaged in a wide variety of biological processes. According to the number of cysteines in their active site, Grx are classified as dithiolic or monothiolic (1-C-Grx). In most organisms, 1-C-Grx are implicated in iron-sulfur cluster (FeS) metabolism and utilize glutathione as cofactor. Trypanosomatids are parasitic protozoa of the order Kinetoplastida, which cause severe diseases in humans and domestic animals. These parasites exploit a unique thiol-dependent redox system based on bis(glutathionyl)spermidine (trypanothione) rather than on glutathione. Mitochondrial 1-C-Grx1 from trypanosomes differs from orthologues in several features including the use of trypanothione as ligand for FeS binding and the presence of a parasite-specific N-terminal extension. We have recently shown that 1-C-Grx1 from Trypanosoma brucei is indispensable for parasite survival in mouse, making this protein a potential drug target candidate against trypanosomiasis. However, structural information for the full-length form of 1-C-Grx1 is still lacking. Here, we report the NMR resonance assignment of the mature form of Tb1-C-Grx1 including an N-terminal tail, paving the way to disclose the role of this intrinsically disordered region in the protein function.
      PubDate: 2014-05-16
       
  • 1H,        class="a-plus-plus">15N and        class="a-plus-plus">13C Backbone resonance
           assignments of murine met-neuroglobin, free and in complex with cyanide
    • Abstract: Abstract Neuroglobin is a globin present in the brain and retina of mammals. This hexacoordinated hemoprotein binds small diatomic molecules, albeit with lower affinity compared with other globins. We report here the resonance assignment of murine met-Neuroglobine, free and in complex with cyanide.
      PubDate: 2014-05-16
       
  • 1H,        class="a-plus-plus">15N and        class="a-plus-plus">13C resonance assignments for
           3rC and 3rCWP: amyloidogenic variants of imunoglobulin λ 3
           light-chain
    • Abstract: Abstract Primary amyloidosis (AL) is the most common amyloid systemic disease and it is characterized by the deposition of immunoglobulin light-chain amyloid fibers in different organs, causing organ failure. The germ-line lambda 3 immunoglobulin light-chain proteins have been correlated with the AL condition. Two mutants have been derived from this germ-line, the single mutant C34Y (3rC) and the triple mutant C34Y, W35A and P7D (3rCWP), presenting a remarkable difference in amyloid fibril formation propensities in vitro. Here we report the 1H, 13C and 15N resonance assignments of these proteins, as the first step to use solution nuclear magnetic resonance spectroscopy to get a better understanding of the amyloid fibril formation differences between these two mutants.
      PubDate: 2014-05-11
       
  • Resonance assignment and secondary structure determination of full length
           human Dickkopf 4 (hDkk4), a secreted, disulphide-rich Wnt inhibitor
           protein
    • Abstract: Abstract A number of proteins have been shown to modulate canonical Wnt signalling at the cell surface, including members of the Dickkopf (Dkk) family (Baron and Rawadi in J Endocrinol 148:2635–2643, 2007; Cruciat and Niehrs in Cold Spring Harb Perspect Biol 5:a015081, 2013). The Dkk family includes four secreted proteins (Dkk1-4), which are characterised by two highly conserved cysteine-rich regions corresponding to C24–C73 and C128–C201 in human Dkk4 (hDkk4). Here we report essentially complete backbone and comprehensive side chain 15N, 13C and 1H NMR assignments for full length mature hDkk4 (M1–L207) containing a short C-terminal hexa-histidine tag (E208–H222). Analysis of the backbone chemical shift data obtained indicates that there is a very limited amount of regular secondary structure, with only small stretches of β-strand identified in both cysteine-rich regions. The N-terminal region of hDkk4 (M1–G21) and the relatively long linker between the two cysteine-rich regions (E77–Q123) appear to be unstructured and relatively mobile.
      PubDate: 2014-05-11
       
  • 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
       
  • Polypeptide backbone, C       class="a-plus-plus">β and methyl group
           resonance assignments of the 24 kDa plectin repeat domain 6 from
           human protein plectin
    • Abstract: Abstract The 500 kDa protein plectin is essential for the cytoskeletal organization of most mammalian cells and it is up-regulated in some types of cancer. Here, we report nearly complete sequence-specific polypeptide backbone, 13Cβ and methyl group resonance assignments for 24 kDa human plectin(4403–4606) containing the C-terminal plectin repeat domain 6.
      PubDate: 2014-04-11
       
  • NMR backbone resonance assignments of the N, P domains of CopA, a
           copper-transporting ATPase, in the apo and ligand bound states
    • Abstract: Abstract Copper-transporting ATPase, a member of P-type ATPase family, plays a key role in the homeostasis of cellular copper levels. Here, the backbone assignments of the directly connected N and P domains (292 residues, 31 kDa) of Cu-transporting ATPase in the ligand free and the AMPPCP-bound states are reported in solution. The NMR assignments pave the way for binding and dynamics studies of this enzyme to better understand its function.
      PubDate: 2014-04-05
       
  • 13C,        class="a-plus-plus">15N and        class="a-plus-plus">1H resonance assignments of
           receiver domain of ethylene receptor ETR1
    • Abstract: Abstract Ethylene plays versatile functions in regulating plant physiology. Although the high affinity ethylene receptor and its downstream regulators have been identified, the molecular recognition of the receptor interacting domains remains to be established. It has been speculated that the cytoplasmic signaling of the ethylene receptor is a two-component regulatory system involving the conserved receiver domain (RD). Here, we report the NMR chemical shift assignments for RD from Arabidopsis thaliana ethylene receptor ETR1. Nearly complete backbone and side-chain assignments were achieved at pH 6.0 and 25 °C. The assignments and backbone dynamics revealed the secondary structure and showed that ETR1-RD is a monomer in solution. These results will make it possible to monitor downstream binding partners and elucidates our understanding of phosphotransfer in the plant two-component regulatory system in the ethylene signaling pathway.
      PubDate: 2014-04-03
       
  • Solution NMR assignment of LpoB, an outer-membrane anchored
           Penicillin-Binding Protein activator from        class="a-plus-plus">Escherichia coli
    • Abstract: Abstract Bacteria surround their cytoplasmic membrane with the essential heteropolymer peptidoglycan (PG), which is made of glycan chains cross-linked by short peptides, to maintain osmotic stability and cell shape. PG is assembled from lipid II precursor by glycosyltransferase and transpeptidase reactions catalyzed by PG synthases, which are anchored to the cytoplasmic membrane and are controlled from inside the cell by cytoskeletal elements. Recently, two lipoproteins, LpoA and LpoB, were shown to be required in Escherichia coli for activating the main peptidoglycan synthases, Penicillin-Binding Proteins 1A and 1B, from the outer membrane. Here we present the backbone and side-chain assignment of the 1H, 13C and 15N resonances of LpoB from E. coli. We also provide evidence for a two-domain organization of LpoB and a largely disordered, 64 amino acid-long N-terminal domain.
      PubDate: 2014-04-02
       
  • Sequence-specific backbone        class="a-plus-plus">1H,        class="a-plus-plus">13C and        class="a-plus-plus">15N assignments of the
           catalytic domain of the        class="a-plus-plus">Escherichia coli protein
           tyrosine kinase, Wzc
    • Abstract: Abstract Protein tyrosine kinases in bacteria are structurally and functionally distinct from their eukaryotic counterparts. The largest family of bacterial tyrosine kinases, the BY-kinase family, is highly conserved in Gram-negative and Gram-positive species, and plays a central role in biofilm and capsule formation. In Escherichia coli the BY-kinase, Wzc, is a critical component of the machinery responsible for the synthesis and export of the exo-polysaccharide colanic acid, a key constituent of biofilms. Here we present the main-chain 1HN, 15N, 13C′ and 13Cα, side-chain 13Cβ resonance assignments for a construct that encodes the entire 274-residue cytosolic catalytic domain of Wzc.
      PubDate: 2014-04-01
       
  • Solid-state NMR sequential assignments of the C-terminal oligomerization
           domain of human C4b-binding protein
    • Abstract: Abstract The complement 4 binding protein (C4bp) plays a crucial role in the inhibition of the complement cascade. It has an extraordinary seven-arm octopus-like structure with 7 tentacle-like identical chains, held together at their C-terminal end. The C-terminal domain does oligomerize in isolation, and is necessary and sufficient to oligomerize full-length C4bp. It is predicted to form a seven-helix coiled coil, and its multimerization properties make it a promising vaccine adjuvant, probably by enhancing the structural stability and binding affinity of the presented antigen. Here, we present the solid-state NMR resonance assignment of the human C4bp C-terminal oligomerization Domain, hC4pbOD, and the corresponding secondary chemical shifts.
      PubDate: 2014-04-01
       
  • Protein chemical shift assignments of the unbound and RNA-bound forms of
           the alternative splicing factor SUP-12 from        class="a-plus-plus">C. elegans
    • Abstract: Abstract The splicing factor SUP-12 from Caenorhabditis elegans binds to regulatory RNA elements in pre-mRNA in order to generate tissue-specific alternative splicing for genes such as the fibroblast growth factor receptor egl-15. In nematode muscle cells, SUP-12 promotes the use of a mutually exclusive exon to impart variant binding specificity to the EGL-15 extracellular protein domain. Here we report the side chain and backbone 1H, 13C and 15N chemical shift assignments for the bacterially expressed RNA recognition motif domain from SUP-12, both in isolation as well as bound to a short RNA derived from the intron sequence between exon 4 and exon 5B of egl-15. Comparison of protein chemical shift values for both the backbone and side chain nuclei, coupled with secondary chemical shift analysis, reveal initial details of the RNA recognition.
      PubDate: 2014-04-01
       
  • Backbone 1H,        class="a-plus-plus">13C,        class="a-plus-plus">15N NMR assignments of yeast
           OMP synthase in unliganded form and in complex with orotidine
           5′-monophosphate
    • Abstract: Abstract The type I phosphoribosyltransferase OMP synthase (EC 2.4.2.10) is involved in de novo synthesis of pyrimidine nucleotides forming the UMP precursor orotidine 5′-monophosphate (OMP). The homodimeric enzyme has a Rossman α/β core topped by a base-enclosing “hood” domain and a flexible domain-swapped catalytic loop. High-resolution X-ray structures of the homologous Salmonella typhimurium and yeast enzymes show that a general compacting of the core as well as movement of the hood and a major disorder-to-order transition of the loop occur upon binding of ligands MgPRPP and orotate. Here we present backbone NMR assignments for the unliganded yeast enzyme (49 kDa) and its complex with product OMP. We were able to assign 212–213 of the 225 non-proline backbone 15N and amide proton resonances. Significant difference in chemical shifts of the amide cross peaks occur in regions of the structure that undergo movement upon ligand occupancy in the S. typhimurium enzyme.
      PubDate: 2014-04-01
       
 
 
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