| pubmed-article:7591482 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7591482 | lifeskim:mentions | umls-concept:C0036720 | lld:lifeskim |
| pubmed-article:7591482 | lifeskim:mentions | umls-concept:C0026377 | lld:lifeskim |
| pubmed-article:7591482 | lifeskim:mentions | umls-concept:C1555029 | lld:lifeskim |
| pubmed-article:7591482 | lifeskim:mentions | umls-concept:C0541749 | lld:lifeskim |
| pubmed-article:7591482 | lifeskim:mentions | umls-concept:C1550045 | lld:lifeskim |
| pubmed-article:7591482 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:7591482 | pubmed:dateCreated | 1995-11-27 | lld:pubmed |
| pubmed-article:7591482 | pubmed:abstractText | NMR spectroscopy has been employed for the conformational analysis of the cyclic hexapeptide cyclo(-D-Pro1-Ala2-Ser3(Bzl)-Trp4-Orn5(Z)-Tyr 6-) with and without protecting groups on Ser3 and Orn5. This peptide sequence was derived from the active loop sequence of the alpha-amylase inhibitor Tendamistat (HOE 467). The aim was to investigate the role of serine in position i of a standard beta-turn on the conformation and stabilization of this turn. Based on distance and torsion constraints from 2D NMR spectroscopic measurements in DMSO-d6 solution, structure refinement was accomplished by restrained molecular dynamics (MD) simulations in vacuo and in DMSO. The analysis of both structures in solution reveals a considerable effect of the unprotected serine sidechain on the adjacent beta-turn conformation. While in the protected peptide with Ser3(Bzl) a beta II-turn is observed between Trp4 and Orn5, the deprotected compound reveals a beta I-turn in this region. The beta I-turn is stabilized by a backbone-sidechain hydrogen bond from Orn5N alpha H to Ser3O gamma. Comparisons with other NMR-derived solution structures of cyclic model peptides and in some protein structures from literature reveal a general structural motif in the stabilization of beta I-turns by serine in the i position through backbone-sidechain interactions. | lld:pubmed |
| pubmed-article:7591482 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7591482 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7591482 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7591482 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7591482 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7591482 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7591482 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7591482 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7591482 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7591482 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7591482 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7591482 | pubmed:month | May | lld:pubmed |
| pubmed-article:7591482 | pubmed:issn | 0367-8377 | lld:pubmed |
| pubmed-article:7591482 | pubmed:author | pubmed-author:KesslerHH | lld:pubmed |
| pubmed-article:7591482 | pubmed:author | pubmed-author:MattesKK | lld:pubmed |
| pubmed-article:7591482 | pubmed:author | pubmed-author:GemmeckerGG | lld:pubmed |
| pubmed-article:7591482 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7591482 | pubmed:volume | 45 | lld:pubmed |
| pubmed-article:7591482 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7591482 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7591482 | pubmed:pagination | 430-40 | lld:pubmed |
| pubmed-article:7591482 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
| pubmed-article:7591482 | pubmed:meshHeading | pubmed-meshheading:7591482-... | lld:pubmed |
| pubmed-article:7591482 | pubmed:meshHeading | pubmed-meshheading:7591482-... | lld:pubmed |
| pubmed-article:7591482 | pubmed:meshHeading | pubmed-meshheading:7591482-... | lld:pubmed |
| pubmed-article:7591482 | pubmed:meshHeading | pubmed-meshheading:7591482-... | lld:pubmed |
| pubmed-article:7591482 | pubmed:meshHeading | pubmed-meshheading:7591482-... | lld:pubmed |
| pubmed-article:7591482 | pubmed:meshHeading | pubmed-meshheading:7591482-... | lld:pubmed |
| pubmed-article:7591482 | pubmed:meshHeading | pubmed-meshheading:7591482-... | lld:pubmed |
| pubmed-article:7591482 | pubmed:meshHeading | pubmed-meshheading:7591482-... | lld:pubmed |
| pubmed-article:7591482 | pubmed:meshHeading | pubmed-meshheading:7591482-... | lld:pubmed |
| pubmed-article:7591482 | pubmed:meshHeading | pubmed-meshheading:7591482-... | lld:pubmed |
| pubmed-article:7591482 | pubmed:meshHeading | pubmed-meshheading:7591482-... | lld:pubmed |
| pubmed-article:7591482 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7591482 | pubmed:articleTitle | Influence of serine in position i on conformation and dynamics of reverse turns. | lld:pubmed |
| pubmed-article:7591482 | pubmed:affiliation | Institute of Organic Chemistry and Biochemistry, Technical University of Munich, Garching, Germany. | lld:pubmed |
| pubmed-article:7591482 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7591482 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
