Zobrazeno 1 - 10
of 47
pro vyhledávání: '"Zhengshuang Shi"'
Publikováno v:
Chemical Communications. 54:5764-5767
Hydration is important in many fundamental processes. To investigate hydration effects on peptide conformations, we examined neighboring-residue and side-chain blocking effects in AcLXPNH2. A correlation between two effects suggests that hydration st
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3f46b80e812742f88d86ed071894576c
https://doi.org/10.1039/c8cc02402b
https://doi.org/10.1039/c8cc02402b
Publikováno v:
Chemical Communications
We report here the construction of 3-way and 4-way peptide nucleic acid (PNA) junctions as basic structural units for PNA nanostructuring. The incorporation of amino acid residues into PNA chains makes PNA nanostructures with more structural complexi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7d8ca27d59100ce0ab7c16fb4fde5003
https://doi.org/10.1039/c8cc00108a
https://doi.org/10.1039/c8cc00108a
Autor:
Zhengshuang Shi
Publikováno v:
Journal of Physics: Conference Series. 2033:012175
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::879d68e755bced3a67ec84a67304b1ff
https://doi.org/10.1088/1742-6596/2033/1/012175
https://doi.org/10.1088/1742-6596/2033/1/012175
Publikováno v:
Chemical communications (Cambridge, England). 54(45)
Hydration is important in many fundamental processes. To investigate hydration effects on peptide conformations, we examined neighboring-residue and side-chain blocking effects in AcLXPNH2. A correlation between two effects suggests that hydration st
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b4ecb0465a53a03aeb7478e3ee178b2e
https://pubmed.ncbi.nlm.nih.gov/29781018
https://pubmed.ncbi.nlm.nih.gov/29781018
Publikováno v:
Scientific Reports
Intrinsic backbone conformational preferences of different amino acids are important for understanding the local structure of unfolded protein chains. Recent evidence suggests α-structure is relatively minor among three major backbone conformations
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::90be4b6195b4e40edab10dee40b224f8
Publikováno v:
Journal of the American Chemical Society. 134:1571-1576
Previously, we derived a P(II) propensity scale using N- and C-terminally blocked host-guest peptide model AcGGXGGNH(2) (X ≠ Gly) and concluded that P(II) represents a dominant conformation in the majority of this series of 19 peptides (Shi et al.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fb0c173002399f52ec801380dabc273f
https://doi.org/10.1021/ja2070363
https://doi.org/10.1021/ja2070363
Publikováno v:
Amino Acids, Peptides and Proteins in Organic Chemistry: Protection Reactions, Medicinal Chemistry, Combinatorial Synthesis, Volume 4
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::938b54eccc0027d34f5e625e781b791c
https://doi.org/10.1002/9783527631827.ch15
https://doi.org/10.1002/9783527631827.ch15
Publikováno v:
Current Opinion in Structural Biology. 16:686-692
The allosteric regulation of protein kinases serves as an efficient strategy for molecular communication, event coupling and interconversion between catalytic states. Recent co-crystal structures have revealed novel ways in which kinases control acti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3858b00fe14b50fcc7eea50d1bbb16be
https://doi.org/10.1016/j.sbi.2006.10.011
https://doi.org/10.1016/j.sbi.2006.10.011
Publikováno v:
Proceedings of the National Academy of Sciences. 102:17964-17968
There is growing appreciation of the functional relevance of unfolded proteins in biology. However, unfolded states of proteins have proven inaccessible to the usual techniques for high-resolution structural and energetic characterization. Unfolded s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c7d223bee51f685b5ecb5ebdfb584578
https://doi.org/10.1073/pnas.0507124102
https://doi.org/10.1073/pnas.0507124102
Publikováno v:
Langmuir. 21:10632-10637
Sodium bis(2-ethylhexyl)sulfosuccinate (AOT) is a surfactant commonly used to encapsulate water soluble proteins within the aqueous core of a reverse micelle. In the context of high-resolution NMR studies of encapsulated proteins the size of the resu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c3665e466270f7575063de66827cadbc
https://doi.org/10.1021/la051409a
https://doi.org/10.1021/la051409a