{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,9,3]],"date-time":"2025-09-03T09:54:13Z","timestamp":1756893253393,"version":"3.41.2"},"reference-count":31,"publisher":"Oxford University Press (OUP)","issue":"5","license":[{"start":{"date-parts":[[2021,2,11]],"date-time":"2021-02-11T00:00:00Z","timestamp":1613001600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/open_access\/funder_policies\/chorus\/standard_publication_model"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2021,9,2]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>In this paper, we show that the combination of NMR theoretical and experimental results can help to solve the molecular structure of peptides, here it is used as an example the residue Leucine-67 in Desulfovibrio vulgaris flavodoxin. We apply a computational protocol based on the leucine amino acid dipeptide, which, using calculated and experimental spin\u2013spin coupling constants, allows us to obtain the conformation of the amino acid side chain. Calculated results show that the best agreement is obtained when three conformers around the lateral chain angle $\\chi _1$ are considered or when the dynamic effect in the torsional angles is included. The population of each structure is estimated and analyzed according to the correlation between those two approaches. Independently of the approach, the estimated $\\chi _1$ angle in solution is close to the staggered value of -60$^\\circ $ and deviates significantly from the average x-ray angle of -90$^\\circ $.<\/jats:p>","DOI":"10.1093\/bib\/bbab020","type":"journal-article","created":{"date-parts":[[2021,1,15]],"date-time":"2021-01-15T00:17:55Z","timestamp":1610669875000},"source":"Crossref","is-referenced-by-count":3,"title":["Computational approaches to amino acid side-chain conformation using combined NMR theoretical and experimental results: leucine-67 in <i>Desulfovibrio vulgaris<\/i> flavodoxin"],"prefix":"10.1093","volume":"22","author":[{"given":"Jes\u00fas","family":"San Fabi\u00e1n","sequence":"first","affiliation":[{"name":"Departamento de Qu\u00edmica F\u00edsica Aplicada, Universidad Aut\u00f3noma de Madrid, Facultad de Ciencias, 28049, Madrid, Spain"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Salama","family":"Omar","sequence":"additional","affiliation":[{"name":"Departamento de Qu\u00edmica F\u00edsica Aplicada, Universidad Aut\u00f3noma de Madrid, Facultad de Ciencias, 28049, Madrid, Spain"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jos\u00e9 Manuel","family":"Garc\u00eda de la Vega","sequence":"additional","affiliation":[{"name":"Departamento de Qu\u00edmica F\u00edsica Aplicada, Universidad Aut\u00f3noma de Madrid, Facultad de Ciencias, 28049, Madrid, Spain"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"286","published-online":{"date-parts":[[2021,2,11]]},"reference":[{"key":"2021090815140230400_ref1","first-page":"482","article-title":"Sixty-five years of the long march in protein secondary structure prediction: the final stretch?","volume":"19","author":"Yang","year":"2018","journal-title":"Brief Bioinform"},{"key":"2021090815140230400_ref2","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1146\/annurev-biophys-070317-032838","article-title":"Transition of proteins and the interplay between backbone, sidechain and solvent interactions","volume":"47","author":"Holehouse","year":"2018","journal-title":"Annu Rev Biophys"},{"key":"2021090815140230400_ref3","doi-asserted-by":"crossref","first-page":"D506","DOI":"10.1093\/nar\/gky1049","article-title":"Uniprot: a worldwide hub of protein knowledge","volume":"47","author":"The UniProt Consortium","year":"2019","journal-title":"Nucleic Acids Res"},{"key":"2021090815140230400_ref4","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1063\/1.1729860","article-title":"Contact electro-spin coupling of nuclear magnetic moments","volume":"30","author":"Karplus","year":"1959","journal-title":"J Chem Phys"},{"key":"2021090815140230400_ref5","doi-asserted-by":"crossref","first-page":"2870","DOI":"10.1021\/ja00901a059","article-title":"Vicinal proton coupling in nuclear magnetic resonance","volume":"85","author":"Karplus","year":"1963","journal-title":"J Am Chem Soc"},{"key":"2021090815140230400_ref6","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1016\/B978-0-12-800185-1.00005-X","article-title":"Dependencies of J-couplings upon dihedral angles on proteins","volume":"81","author":"Salvador","year":"2014","journal-title":"Annu Rep NMR Spectrosc"},{"key":"2021090815140230400_ref7","doi-asserted-by":"crossref","first-page":"7081","DOI":"10.1021\/ja003724j","article-title":"Self-consistent Karplus parametrization of ${}^3$J coupling depending on the polypeptide side-chain torsion ${\\chi }\\_1$","volume":"123","author":"P\u00e9rez","year":"2001","journal-title":"J Am Chem Soc"},{"key":"2021090815140230400_ref8","first-page":"287","article-title":"Asymmetric Karplus curves for the protein side-chain ${}^3$J couplings","volume-title":"J Biomol NMR","author":"Schmidt","year":"2007"},{"key":"2021090815140230400_ref9","doi-asserted-by":"crossref","first-page":"5648","DOI":"10.1063\/1.464913","article-title":"Density-functional thermochemistry. iii. 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