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1 Ramachandran criticizes Trivers' conjecture, arguing tha
2 Ramachandran et al. argued that ICC neurons of types V,
3 Ramachandran scores and other geometric indicators show
4 nstrate that this sensitivity results from a Ramachandran dihedral psi angle dependent coupling of th
9 es can be depicted graphically to provide a 'Ramachandran'-type view of RNA global structure that can
11 e relationship between Raman frequencies and Ramachandran dihedral angles of the polypeptide backbone
15 ctures, based upon empirical metrics such as Ramachandran geometries and chi(1)/chi(2) distributions,
16 s for a statistical mapping of the available Ramachandran space of each amino acid in terms of confor
17 tions and during the transit process between Ramachandran basins, e.g., from the beta to the alpha re
19 can be mapped in two dimensions, as shown by Ramachandran, Sasisekharan, and Ramakrishnan almost half
20 oups based on the clusters from the complete Ramachandran data: nonpolar/beta-branched (Ile and Val),
24 this increase to be the result of different Ramachandran angle values in certain residues of the Abe
25 We lastly postulate that these different Ramachandran angle values could possibly be traced to th
26 e further illuminated in three-dimensional, "Ramachandran-type" plots that relate D-B and B-A torsion
27 its time-dependent sequences of discretized Ramachandran basins occupied by successive backbone resi
28 utions of main chain (Phi,Psi) angles (i.e., Ramachandran maps) of the 20 naturally occurring amino a
29 approximated as hard spheres, the eponymous Ramachandran plot demonstrated that steric clashes alone
30 rs, identification of possible model errors, Ramachandran-style conformational maps and classificatio
31 final structures of the dimer had favorable Ramachandran angles and a root-mean-square deviation of
32 als alternate between left- and right-handed Ramachandran angles, which also justifies the need for c
42 to correlate structure and observed potency, Ramachandran-type plots were calculated for a series of
44 mperature dependence of the peptide bond Psi Ramachandran angle population distribution of a 21-resid
45 a method to estimate the distribution of Psi Ramachandran angles for these conformations, which we us
47 ndence of the amide frequencies on their Psi Ramachandran angles and hydrogen bonding enables us, for
50 ative Gibbs free energy landscapes along the Ramachandran Psi-coordinate of a mainly poly-Ala peptide
51 lts on the conformational equilibria and the Ramachandran Psi angle (un)folding Gibbs free energy lan
55 We describe a new method to estimate the Ramachandran Psi-angular distributions from amide III ba
57 e PPII and right-handed helix troughs in the Ramachandran plot, which is part of the very heterogeneo
58 ional Gaussian distribution functions in the Ramachandran space pertaining to subensembles of polypro
60 an force in the extended chain region of the Ramachandran diagram, which broadens as the temperature
66 dihedral angles lie in the right side of the Ramachandran plot (alpha(L) region; phi 97 degrees).
67 handed alpha-helical region (L-alpha) of the Ramachandran plot are a potential indicator of structura
68 es of amino acids in specific regions of the Ramachandran plot are preferred at the functional sites
69 many residues lie in the beta-region of the Ramachandran plot, and molecular-dynamics simulations co
70 ning the extended and helical regions of the Ramachandran plot, and they detect a predominant average
73 s possible within the allowed regions of the Ramachandran space with only minor mutations to a known
74 eta-structure, and PPII-helix regions of the Ramachandran surface and that they "flicker" between the
76 ued our development of methods to relate the Ramachandran Psi-angle to the amide III band frequency.
77 The obtained values are very close to the Ramachandran coordinates of the polyproline II helix (PP
78 rently reporting on backbone sampling within Ramachandran substates, while a slower component (5-25 n
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