Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Tommi Hassinen"'
Autor:
Pekka Poutiainen, Pasi Soininen, Juuso Lehtivarjo, Pekka Laatikainen, Mika Tiainen, Olli Jääskeläinen, Reino Laatikainen, Tommi Hassinen, Samuli-Petrus Korhonen, Tuulia Tynkkynen, Topi K. Väisänen, Henri Martonen, Juha Jungman, Janne Weisell, Matthias Niemitz, Kari Tuppurainen
Publikováno v:
Journal of Chemical Information and Modeling. 54(2):419-430
A fast 3D/4D structure-sensitive procedure was developed and assessed for the chemical shift prediction of protons bonded to sp3carbons, which poses the maybe greatest challenge in the NMR spectral parameter prediction. The LPNC (Linear Prediction wi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::720e28b2c56613d89702a724c04f4478
http://juuli.fi/Record/0028707214
http://juuli.fi/Record/0028707214
1H NMR spectral analysis and conformational behavior of n-alkanes in different chemical environments
Publikováno v:
Magnetic Resonance in Chemistry. 50:598-607
Alkyl chains are common structural units, for example in lipids, and their 1H NMR spectral parameters offer valuable information about their conformational behavior in solvent environment. Even the spectra of short n-alkanes are complex, which is obv
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::55ee0d679963b55f7b10b6941918a594
https://doi.org/10.1002/mrc.3847
https://doi.org/10.1002/mrc.3847
Publikováno v:
Journal of Biomolecular NMR. 52:257-267
While chemical shifts are invaluable for obtaining structural information from proteins, they also offer one of the rare ways to obtain information about protein dynamics. A necessary tool in transforming chemical shifts into structural and dynamic i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8b6253774205cd84da4ef011ba0117e0
https://doi.org/10.1007/s10858-012-9609-6
https://doi.org/10.1007/s10858-012-9609-6
Autor:
Tommi Hassinen, Mikael Peräkylä
Publikováno v:
Journal of Computational Chemistry. 22:1229-1242
Parameterization and test calculations of a reduced protein model with new energy terms are presented. The new energy terms retain the steric properties and the most significant degrees of freedom of protein side chains in an efficient way using only
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fe3ead3967c904e7e5a6d08bd2d8e58a
https://doi.org/10.1002/jcc.1080
https://doi.org/10.1002/jcc.1080
Autor:
Jouko Vepsäläinen, Ursula Weber, Reino Laatikainen, Tommi Hassinen, Matthias Niemitz, Jukka Sundelin
Publikováno v:
Journal of Magnetic Resonance, Series A. 120:1-10
Strategies for spectral analysis of high-resolution NMR spectra have been examined. In this report, a fast algorithm based on the use of integral transforms is also described. The method was developed and tuned with a special emphasis on analysis of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e74c8a561d57f95b4a7f68f1a9b50f39
https://doi.org/10.1006/jmra.1996.0094
https://doi.org/10.1006/jmra.1996.0094
Publikováno v:
Magnetic resonance in chemistry : MRC. 50(9)
Alkyl chains are common structural units, for example in lipids, and their (1) H NMR spectral parameters offer valuable information about their conformational behavior in solvent environment. Even the spectra of short n-alkanes are complex, which is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::a8e7c1915bca69c3a2ac30ee83dc090e
https://pubmed.ncbi.nlm.nih.gov/22829172
https://pubmed.ncbi.nlm.nih.gov/22829172
Publikováno v:
Journal of biomolecular NMR. 45(4)
A 4D approach for protein 1H chemical shift prediction was explored. The 4th dimension is the molecular flexibility, mapped using molecular dynamics simulations. The chemical shifts were predicted with a principal component model based on atom coordi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::51397407fa12b615d93fc5031d0c52b8
https://pubmed.ncbi.nlm.nih.gov/19876601
https://pubmed.ncbi.nlm.nih.gov/19876601
Publikováno v:
Protein engineering. 15(8)
Free energies of the alpha(r)beta and betabeta conformations of 14 tetrapeptides, based on the sequence SALN and protein X-ray structures, were calculated using molecular dynamics simulations and MM-PBSA calculations. The alphaalpha conformations of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::031fac6a4ece6bf3b632db1c362603de
https://pubmed.ncbi.nlm.nih.gov/12364579
https://pubmed.ncbi.nlm.nih.gov/12364579
Publikováno v:
Biophysical chemistry. 73(1-2)
Principal component analysis (PCA) of molecular dynamics simulations of hen egg white lysozyme and its mutants indicate that even small changes in the amino acid sequence alter considerably the internal molecular motions and that the internal motions
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cc91cf92d9134d70d37827122dfe6f15
https://pubmed.ncbi.nlm.nih.gov/9697297
https://pubmed.ncbi.nlm.nih.gov/9697297