Sökning: onr:"swepub:oai:gup.ub.gu.se/228427" > The Impact of Inter...
Fältnamn | Indikatorer | Metadata |
---|---|---|
000 | 03827naa a2200505 4500 | |
001 | oai:gup.ub.gu.se/228427 | |
003 | SwePub | |
008 | 240528s2015 | |||||||||||000 ||eng| | |
009 | oai:DiVA.org:uu-356019 | |
024 | 7 | a https://gup.ub.gu.se/publication/2284272 URI |
024 | 7 | a https://doi.org/10.1002/bip.226712 DOI |
024 | 7 | a https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-3560192 URI |
040 | a (SwePub)gud (SwePub)uu | |
041 | a eng | |
042 | 9 SwePub | |
072 | 7 | a ref2 swepub-contenttype |
072 | 7 | a art2 swepub-publicationtype |
100 | 1 | a Niebling, Stephanu Gothenburg University,Göteborgs universitet,Institutionen för kemi och molekylärbiologi,Department of Chemistry and Molecular Biology4 aut |
245 | 1 0 | a The Impact of Interchain Hydrogen Bonding on b-Hairpin Stability is Readily Predicted by Molecular Dynamics Simulation |
264 | c 2015-11-26 | |
264 | 1 | b Wiley,c 2015 |
520 | a Peptides are frequently used model systems for protein folding. They are also gaining increased importance as therapeutics. Here, the ability of molecular dynamics (MD) simulation for describing the structure and dynamics of β-hairpin peptides was investigated, with special attention given to the impact of a single interstrand sidechain to sidechain interaction. The MD trajectories were compared to structural information gained from solution NMR. By assigning frames from restraint-free MD simulations to an intuitive hydrogen bond on/off pattern, folding ratios and folding pathways were predicted. The computed molecular model successfully reproduces the folding ratios determined by NMR, indicating that MD simulation may be straightforwardly used as a screening tool in β-hairpin design. | |
650 | 7 | a MEDICIN OCH HÄLSOVETENSKAPx Medicinska och farmaceutiska grundvetenskaperx Andra medicinska och farmaceutiska grundvetenskaper0 (SwePub)301992 hsv//swe |
650 | 7 | a MEDICAL AND HEALTH SCIENCESx Basic Medicinex Other Basic Medicine0 (SwePub)301992 hsv//eng |
650 | 7 | a MEDICIN OCH HÄLSOVETENSKAPx Medicinska och farmaceutiska grundvetenskaperx Läkemedelskemi0 (SwePub)301032 hsv//swe |
650 | 7 | a MEDICAL AND HEALTH SCIENCESx Basic Medicinex Medicinal Chemistry0 (SwePub)301032 hsv//eng |
650 | 7 | a NATURVETENSKAPx Kemix Organisk kemi0 (SwePub)104052 hsv//swe |
650 | 7 | a NATURAL SCIENCESx Chemical Sciencesx Organic Chemistry0 (SwePub)104052 hsv//eng |
653 | a peptid | |
653 | a hairpin | |
653 | a folding | |
653 | a molecular dynamics | |
653 | a hydrogen bond | |
653 | a conformation | |
653 | a beta-hairpin | |
700 | 1 | a Danelius, Emmau Gothenburg University,Göteborgs universitet,Institutionen för kemi och molekylärbiologi,Department of Chemistry and Molecular Biology4 aut |
700 | 1 | a Brath, Ulrikau Gothenburg University,Göteborgs universitet,Institutionen för kemi och molekylärbiologi,Department of Chemistry and Molecular Biology4 aut0 (Swepub:gu)xbraul |
700 | 1 | a Westenhoff, Sebastian,d 1978u Gothenburg University,Göteborgs universitet,Institutionen för kemi och molekylärbiologi,Department of Chemistry and Molecular Biology4 aut0 (Swepub:gu)xwests |
700 | 1 | a Erdelyi, Mate,d 1975u Gothenburg University,Göteborgs universitet,Institutionen för kemi och molekylärbiologi,Department of Chemistry and Molecular Biology,organisk kemi4 aut0 (Swepub:uu)mateerde |
710 | 2 | a Göteborgs universitetb Institutionen för kemi och molekylärbiologi4 org |
773 | 0 | t Peptide Scienced : Wileyg 104:6, s. 703-706q 104:6<703-706x 1097-0282x 0006-3525 |
856 | 4 | u https://onlinelibrary.wiley.com/doi/pdfdirect/10.1002/bip.22671 |
856 | 4 8 | u https://gup.ub.gu.se/publication/228427 |
856 | 4 8 | u https://doi.org/10.1002/bip.22671 |
856 | 4 8 | u https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-356019 |
Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.