| pubmed-article:21388199 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:21388199 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:21388199 | lifeskim:mentions | umls-concept:C1519249 | lld:lifeskim |
| pubmed-article:21388199 | lifeskim:mentions | umls-concept:C1516769 | lld:lifeskim |
| pubmed-article:21388199 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:21388199 | lifeskim:mentions | umls-concept:C1880157 | lld:lifeskim |
| pubmed-article:21388199 | lifeskim:mentions | umls-concept:C1707689 | lld:lifeskim |
| pubmed-article:21388199 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:21388199 | pubmed:dateCreated | 2011-3-23 | lld:pubmed |
| pubmed-article:21388199 | pubmed:abstractText | The de novo design of protein-binding peptides is challenging because it requires the identification of both a sequence and a backbone conformation favorable for binding. We used a computational strategy that iterates between structure and sequence optimization to redesign the C-terminal portion of the RGS14 GoLoco motif peptide so that it adopts a new conformation when bound to G?(i1). An X-ray crystal structure of the redesigned complex closely matches the computational model, with a backbone root-mean-square deviation of 1.1 Å. | lld:pubmed |
| pubmed-article:21388199 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21388199 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21388199 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21388199 | pubmed:language | eng | lld:pubmed |
| pubmed-article:21388199 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21388199 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:21388199 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21388199 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21388199 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:21388199 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:21388199 | pubmed:issn | 1520-5126 | lld:pubmed |
| pubmed-article:21388199 | pubmed:author | pubmed-author:SiderovskiDav... | lld:pubmed |
| pubmed-article:21388199 | pubmed:author | pubmed-author:KuhlmanBrianB | lld:pubmed |
| pubmed-article:21388199 | pubmed:author | pubmed-author:MachiusMischa... | lld:pubmed |
| pubmed-article:21388199 | pubmed:author | pubmed-author:SammondDeanne... | lld:pubmed |
| pubmed-article:21388199 | pubmed:author | pubmed-author:ButterfossGle... | lld:pubmed |
| pubmed-article:21388199 | pubmed:author | pubmed-author:PurbeckCarrie... | lld:pubmed |
| pubmed-article:21388199 | pubmed:author | pubmed-author:BoschDustin... | lld:pubmed |
| pubmed-article:21388199 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:21388199 | pubmed:day | 30 | lld:pubmed |
| pubmed-article:21388199 | pubmed:volume | 133 | lld:pubmed |
| pubmed-article:21388199 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:21388199 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:21388199 | pubmed:pagination | 4190-2 | lld:pubmed |
| pubmed-article:21388199 | pubmed:meshHeading | pubmed-meshheading:21388199... | lld:pubmed |
| pubmed-article:21388199 | pubmed:meshHeading | pubmed-meshheading:21388199... | lld:pubmed |
| pubmed-article:21388199 | pubmed:meshHeading | pubmed-meshheading:21388199... | lld:pubmed |
| pubmed-article:21388199 | pubmed:meshHeading | pubmed-meshheading:21388199... | lld:pubmed |
| pubmed-article:21388199 | pubmed:meshHeading | pubmed-meshheading:21388199... | lld:pubmed |
| pubmed-article:21388199 | pubmed:meshHeading | pubmed-meshheading:21388199... | lld:pubmed |
| pubmed-article:21388199 | pubmed:meshHeading | pubmed-meshheading:21388199... | lld:pubmed |
| pubmed-article:21388199 | pubmed:meshHeading | pubmed-meshheading:21388199... | lld:pubmed |
| pubmed-article:21388199 | pubmed:year | 2011 | lld:pubmed |
| pubmed-article:21388199 | pubmed:articleTitle | Computational design of the sequence and structure of a protein-binding peptide. | lld:pubmed |
| pubmed-article:21388199 | pubmed:affiliation | Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, North Carolina 27599-7260, USA. | lld:pubmed |
| pubmed-article:21388199 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:21388199 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:21388199 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
