| http://purl.uniprot.org/citations/15368576 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15368576 | http://www.w3.org/2000/01/rdf-schema#comment | "HEV32, a 32-residue, truncated hevein lacking eleven C-terminal amino acids, was synthesized by solid-phase methodology and correctly folded with three cysteine bridge pairs. The affinities of HEV32 for small chitin fragments--in the forms of N,N',N"-triacetylchitotriose ((GlcNAc)3) (millimolar) and N,N',N",N"',N"",N""'-hexaacetylchitohexaose ((GlcNAc)6) (micromolar)--as measured by NMR and fluorescence methods, are comparable with those of native hevein. The HEV32 ligand-binding process is enthalpy driven, while entropy opposes binding. The NMR structure of ligand-bound HEV32 in aqueous solution was determined to be highly similar to the NMR structure of ligand-bound hevein. Solvated molecular-dynamics simulations were performed in order to monitor the changes in side-chain conformation of the binding site of HEV32 and hevein upon interaction with ligands. The calculations suggest that the Trp21 side-chain orientation of HEV32 in the free form differs from that in the bound state; this agrees with fluorescence and thermodynamic data. HEV32 provides a simple molecular model for studying protein-carbohydrate interactions and for understanding the physiological relevance of small native hevein domains lacking C-terminal residues."xsd:string |
| http://purl.uniprot.org/citations/15368576 | http://purl.org/dc/terms/identifier | "doi:10.1002/cbic.200400025"xsd:string |
| http://purl.uniprot.org/citations/15368576 | http://purl.uniprot.org/core/author | "Jimenez-Barbero J."xsd:string |
| http://purl.uniprot.org/citations/15368576 | http://purl.uniprot.org/core/author | "Asensio J.L."xsd:string |
| http://purl.uniprot.org/citations/15368576 | http://purl.uniprot.org/core/author | "Andreu D."xsd:string |
| http://purl.uniprot.org/citations/15368576 | http://purl.uniprot.org/core/author | "Groves P."xsd:string |
| http://purl.uniprot.org/citations/15368576 | http://purl.uniprot.org/core/author | "Canada F.J."xsd:string |
| http://purl.uniprot.org/citations/15368576 | http://purl.uniprot.org/core/author | "Aboitiz N."xsd:string |
| http://purl.uniprot.org/citations/15368576 | http://purl.uniprot.org/core/author | "Vila-Perello M."xsd:string |
| http://purl.uniprot.org/citations/15368576 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/15368576 | http://purl.uniprot.org/core/name | "Chembiochem"xsd:string |
| http://purl.uniprot.org/citations/15368576 | http://purl.uniprot.org/core/pages | "1245-1255"xsd:string |
| http://purl.uniprot.org/citations/15368576 | http://purl.uniprot.org/core/title | "NMR and modeling studies of protein-carbohydrate interactions: synthesis, three-dimensional structure, and recognition properties of a minimum hevein domain with binding affinity for chitooligosaccharides."xsd:string |
| http://purl.uniprot.org/citations/15368576 | http://purl.uniprot.org/core/volume | "5"xsd:string |
| http://purl.uniprot.org/citations/15368576 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15368576 |
| http://purl.uniprot.org/citations/15368576 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/15368576 |
| http://purl.uniprot.org/uniprot/#_P02877-mappedCitation-15368576 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/15368576 |
| http://purl.uniprot.org/uniprot/#_P27275-mappedCitation-15368576 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/15368576 |
| http://purl.uniprot.org/uniprot/P27275 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/15368576 |
| http://purl.uniprot.org/uniprot/P02877 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/15368576 |