Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Peptide plane flipping"'
Publikováno v:
Journal of Biomolecular Structure and Dynamics. 33:552-562
For the past 50 years, the Ramachandran map has been used effectively to study the protein structure and folding. However, though extensive analysis has been done on dihedral angle preferences of residues in globular proteins, related studies and rep
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eb40aa5c70a17ac1d3a8f04e53d1740d
https://doi.org/10.1080/07391102.2014.895678
https://doi.org/10.1080/07391102.2014.895678
Autor:
William D. Lubell, Caroline Proulx
Publikováno v:
Biopolymers. 102:7-15
N-Amino-imidazolin-2-ones, a new class of turn mimics onto which side chains of different amino acids may be added conveniently, have been analyzed by X-ray crystallography. 4-Methyl and 4-benzyl N-amino-imidazolin-2-one tetrapeptide models 2 and 3 w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::57dc9865010adfd4fe13f39e41bf6ad5
https://doi.org/10.1002/bip.22327
https://doi.org/10.1002/bip.22327
Autor:
Steven Hayward
Publikováno v:
Protein Science. 10:2219-2227
A peptide-plane flip is a large-scale rotation of the peptide plane that takes the phi,psi angles at residues i and i + 1 to different structural regions in the Ramachandran plot with a comparatively small effect on the relative orientation of their
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::96ca41194427ac2910888b1f36958fe6
https://doi.org/10.1110/ps.23101
https://doi.org/10.1110/ps.23101
Publikováno v:
BioMed Research International, Vol 2015 (2015)
BioMed Research International
BioMed Research International
Several secondary structures, such asπ-helix and left-handed helix, have been frequently identified at protein ligand-binding sites. A secondary structure is considered to be constrained to a specific region of dihedral angles. However, a comprehens
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7d87ed42913c0ffe3647dae0f0d7d389
https://doaj.org/article/c3cd72d7fbfc4686a176e04e3f1bc979
https://doaj.org/article/c3cd72d7fbfc4686a176e04e3f1bc979
Publikováno v:
Biochemistry. 46:669-682
To identify basic local backbone motions in unfolded chains, simulations are performed for a variety of peptide systems using three popular force fields and for implicit and explicit solvent models. A dominant "crankshaft-like" motion is found that i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::18b0c7f0a6dbf6a6e79aea037d7d1c82
https://doi.org/10.1021/bi061575x
https://doi.org/10.1021/bi061575x
Publikováno v:
Structure. 14(9):1369-1376
The toxic component of amyloid is not the mature fiber but a soluble prefibrillar intermediate. It has been proposed, from molecular dynamics simulations, that the precursor is composed of alpha sheet, which converts into the beta sheet of mature amy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::87c177cfc65cb7a422cf9d9cef452262
Publikováno v:
Journal of Molecular Biology 2005 (2005): 483–487. doi:10.1016/j.jmb.2005.01.065
info:cnr-pdr/source/autori:Esposito, Luciana; De Simone, Alfonso; Zagari, Adriana; Vitagliano, Luigi./titolo:Correlation between Omega and Psi Dihedral Angles in Protein Structures/doi:10.1016%2Fj.jmb.2005.01.065/rivista:Journal of Molecular Biology/anno:2005/pagina_da:483/pagina_a:487/intervallo_pagine:483–487/volume:2005
info:cnr-pdr/source/autori:Esposito, Luciana; De Simone, Alfonso; Zagari, Adriana; Vitagliano, Luigi./titolo:Correlation between Omega and Psi Dihedral Angles in Protein Structures/doi:10.1016%2Fj.jmb.2005.01.065/rivista:Journal of Molecular Biology/anno:2005/pagina_da:483/pagina_a:487/intervallo_pagine:483–487/volume:2005
The planarity of the peptide group is one of the fundamental features of protein structure that is described in every chemistry and biochemistry textbook. By surveying a dataset of 163 atomic resolution protein structures we here identify the stereoc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::68f8d287037914dbd2eff19f7f62ed90
https://doi.org/10.1016/j.jmb.2005.01.065
https://doi.org/10.1016/j.jmb.2005.01.065
Publikováno v:
Journal of Molecular Structure. 609:115-128
Using a method of the theoretical conformational analysis, a conformational dynamics of the side chains of the amino acid residues of peptide T, a competitor of the human immuno-deficiency virus in the binding to human T cells, was investigated. For
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::abe0d5b915caf9e0beeeeed34dc2b2be
https://doi.org/10.1016/s0022-2860(01)00974-7
https://doi.org/10.1016/s0022-2860(01)00974-7
Autor:
Chang-Ju Yoon, Seonggu Ro, Young-Sang Choi, In-Ae Ahn, Ho-Jin Lee, Kang-Bong Lee, Dongkyu Shin
Publikováno v:
Bioorganic & Medicinal Chemistry. 9:1837-1841
We have attempted to design a model dipeptide (acetyl dipeptide amide, Ac-CA1-CA2--NH(2)) that can adopt specifically typical torsion angles of the beta-I turn (phi(i+1), psi(i+1), phi(i+2), psi(i+2)=-60 degrees, -30 degrees, -90 degrees, 0 degrees )
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::25b4a5b7f5780ef136fec350a341616c
https://doi.org/10.1016/s0968-0896(01)00094-3
https://doi.org/10.1016/s0968-0896(01)00094-3
Autor:
J. M. R. Parker
Publikováno v:
Journal of Computational Chemistry. 20:947-955
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a7ebf7810e42588fd83c6df72d7b27d4
https://doi.org/10.1002/(sici)1096-987x(19990715)20:9<947::aid-jcc6>3.0.co
https://doi.org/10.1002/(sici)1096-987x(19990715)20:9<947::aid-jcc6>3.0.co