| http://purl.uniprot.org/citations/10092854 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10092854 | http://www.w3.org/2000/01/rdf-schema#comment | "Nuclear magnetic resonance (NMR) spectroscopy was used to determine the three dimensional structure of rice nonspecific lipid transfer protein (ns-LTP), a 91 amino acid residue protein belonging to the broad family of plant ns-LTP. Sequence specific assignment was obtained for all but three HN backbone 1H resonances and for more than 95% of the 1H side-chain resonances using a combination of 1H 2D NOESY; TOCSY and COSY experiments at 293 K. The structure was calculated on the basis of four disulfide bridge restraints, 1259 distance constraints derived from 1H-1H Overhauser effects, 72 phi angle restraints and 32 hydrogen-bond restraints. The final solution structure involves four helices (H1: Cys3-Arg18, H2: Ala25-Ala37, H3: Thr41-Ala54 and H4: Ala66-Cys73) followed by a long C-terminal tail (T) with no observable regular structure. N-capping residues (Thr2, Ser24, Thr40), whose side-chain oxygen atoms are involved in hydrogen bonds with i + 3 amide proton additionally stabilize the N termini of the first three helices. The fourth helix involving Pro residues display a mixture of alpha and 3(10) conformation. The rms deviation of 14 final structures with respect to the average structure is 1.14 +/-0.16 A for all heavy atoms (C, N, O and S) and 0.72 +/-0.01 A for the backbone atoms. The global fold of rice ns-LTP is close to the previously published structures of wheat, barley and maize ns-LTPs exhibiting nearly identical pattern of the numerous sequence specific interactions. As reported previously for different four-helix topology proteins, hydrophobic, hydrogen bonding and electrostatic mechanisms of fold stabilization were found for the rice ns-LTP. The sequential alignment of 36 ns-LTP primary structures strongly suggests that there is a uniform pattern of specific long-range interactions (in terms of sequence), which stabilize the fold of all plant ns-LTPs."xsd:string |
| http://purl.uniprot.org/citations/10092854 | http://purl.org/dc/terms/identifier | "doi:10.1046/j.1432-1327.1999.00093.x"xsd:string |
| http://purl.uniprot.org/citations/10092854 | http://purl.uniprot.org/core/author | "Suh S.W."xsd:string |
| http://purl.uniprot.org/citations/10092854 | http://purl.uniprot.org/core/author | "Lee J.Y."xsd:string |
| http://purl.uniprot.org/citations/10092854 | http://purl.uniprot.org/core/author | "Vovelle F."xsd:string |
| http://purl.uniprot.org/citations/10092854 | http://purl.uniprot.org/core/author | "Ptak M."xsd:string |
| http://purl.uniprot.org/citations/10092854 | http://purl.uniprot.org/core/author | "Sodano P."xsd:string |
| http://purl.uniprot.org/citations/10092854 | http://purl.uniprot.org/core/author | "Poznanski J."xsd:string |
| http://purl.uniprot.org/citations/10092854 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/10092854 | http://purl.uniprot.org/core/name | "Eur J Biochem"xsd:string |
| http://purl.uniprot.org/citations/10092854 | http://purl.uniprot.org/core/pages | "692-708"xsd:string |
| http://purl.uniprot.org/citations/10092854 | http://purl.uniprot.org/core/title | "Solution structure of a lipid transfer protein extracted from rice seeds. Comparison with homologous proteins."xsd:string |
| http://purl.uniprot.org/citations/10092854 | http://purl.uniprot.org/core/volume | "259"xsd:string |
| http://purl.uniprot.org/citations/10092854 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10092854 |
| http://purl.uniprot.org/citations/10092854 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/10092854 |
| http://purl.uniprot.org/uniprot/#_Q0IQK9-mappedCitation-10092854 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/10092854 |
| http://purl.uniprot.org/uniprot/Q0IQK9 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/10092854 |