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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
5 aint gives rise to inaccessible regions in a Ramachandran plot.
6                                       Like a Ramachandran plot, clusters of residues appear at discre
7 ll in the standard alpha-helical region of a Ramachandran plot.
8                         Here, we show that a Ramachandran-type plot focusing on the two dihedral angl
9                         A graph not unlike a Ramachandran plot is presented illustrating the various
10 es can be depicted graphically to provide a 'Ramachandran'-type view of RNA global structure that can
11 rowly into two specific regions of the L-Ala Ramachandran map.
12 e relationship between Raman frequencies and Ramachandran dihedral angles of the polypeptide backbone
13 -acids side-chain charges within a motif and Ramachandran plots for each residue.
14  simulated annealing, and chemical shift and Ramachandran refinement.
15 ve game in order to investigate Trivers' and Ramachandran's conjectures.
16 tion of turn structure in BB dihedral-angle (Ramachandran) space.
17 ctures, based upon empirical metrics such as Ramachandran geometries and chi(1)/chi(2) distributions,
18 s for a statistical mapping of the available Ramachandran space of each amino acid in terms of confor
19 tions and during the transit process between Ramachandran basins, e.g., from the beta to the alpha re
20      The populations and transitions between Ramachandran basins are studied for combinations of the
21 te the usefulness of this cross-peptide-bond Ramachandran plot by showing that it captures beta-turn
22 can be mapped in two dimensions, as shown by Ramachandran, Sasisekharan, and Ramakrishnan almost half
23 ssue of the Journal of Biological Chemistry, Ramachandran et al. show that in subtype I-E systems, Ca
24 oups based on the clusters from the complete Ramachandran data: nonpolar/beta-branched (Ile and Val),
25 e angle sampling based on neighbor-dependent Ramachandran probability distributions.
26  a van der Waals energy function and derived Ramachandran plots for each of the amino acids.
27                      The sets of NMR derived Ramachandran angles are assembled in a set of test struc
28  this increase to be the result of different Ramachandran angle values in certain residues of the Abe
29     We lastly postulate that these different Ramachandran angle values could possibly be traced to th
30 e further illuminated in three-dimensional, "Ramachandran-type" plots that relate D-B and B-A torsion
31  its time-dependent sequences of discretized Ramachandran basins occupied by successive backbone resi
32 utions of main chain (Phi,Psi) angles (i.e., Ramachandran maps) of the 20 naturally occurring amino a
33  approximated as hard spheres, the eponymous Ramachandran plot demonstrated that steric clashes alone
34 rs, identification of possible model errors, Ramachandran-style conformational maps and classificatio
35  final structures of the dimer had favorable Ramachandran angles and a root-mean-square deviation of
36 als alternate between left- and right-handed Ramachandran angles, which also justifies the need for c
37 d 99% residues within the allowed regions in Ramachandran plot and - 6.61 Z-score, confirming its rel
38 cribed by conformational angles resulting in Ramachandran plots.
39                               In this issue, Ramachandran et al. report that mutations in the gene en
40 affect a peptide's conformational landscape (Ramachandran space).
41  advanced knowledge of the very broad native Ramachandran basin assignments.
42                   To ensure the precision of Ramachandran plot comparisons, we applied a rigorous Bay
43 leophilic residue into a forbidden region of Ramachandran space.
44 e alpha-helical and extended beta-regions of Ramachandran space.
45                      Building on the work of Ramachandran and Santiago, we develop a model that captu
46        A residue's complete transit from one Ramachandran basin to another, however, occurs in a mann
47        Polysaccharides distorted the peptide Ramachandran angles consistent with the circular dichroi
48 to correlate structure and observed potency, Ramachandran-type plots were calculated for a series of
49 nformations, which we used to estimate a Psi Ramachandran angle energy landscape.
50 mperature dependence of the peptide bond Psi Ramachandran angle population distribution of a 21-resid
51 a method to estimate the distribution of Psi Ramachandran angles for these conformations, which we us
52  and calculate the free energy along the Psi Ramachandran angle secondary folding coordinate.
53 ndence of the amide frequencies on their Psi Ramachandran angles and hydrogen bonding enables us, for
54 lations, energy of structure, ensemble RMSD, Ramachandran distribution, and clashscore.
55                                          The Ramachandran angles for the title compound are obtained
56                                          The Ramachandran plot, ProSA-web, ERRAT, and Verify3D were e
57                                          The Ramachandran scores and the stereochemical quality of th
58 ative Gibbs free energy landscapes along the Ramachandran Psi-coordinate of a mainly poly-Ala peptide
59 lts on the conformational equilibria and the Ramachandran Psi angle (un)folding Gibbs free energy lan
60                                  Because the Ramachandran conformations of GlyB20 and GlyB23 are ordi
61                     Finally, inspired by the Ramachandran plot, we developed a plot of Sm versus Em (
62 uently use this information to determine the Ramachandran torsion angles phi and psi.
63 c features, the new features, especially the Ramachandran basin potential, provide statistical and ev
64     We describe a new method to estimate the Ramachandran Psi-angular distributions from amide III ba
65 ctures and a considerable improvement in the Ramachandran map statistics.
66 e PPII and right-handed helix troughs in the Ramachandran plot, which is part of the very heterogeneo
67 ional Gaussian distribution functions in the Ramachandran space pertaining to subensembles of polypro
68                                     Like the Ramachandran plot, the eta-theta plot is a valuable syst
69 an force in the extended chain region of the Ramachandran diagram, which broadens as the temperature
70                      Further analysis of the Ramachandran dihedral angles (phi, psi) reveals that the
71 D' for alpha regions on the left side of the Ramachandran map and 'a' and 'd' for equivalent regions
72 la)(n) conformers in the P(II) region of the Ramachandran map.
73 about residue occupancy in any region of the Ramachandran map.
74 oline II region to the helical region of the Ramachandran map.
75 unhindered by the chiral restrictions of the Ramachandran plane.
76 dihedral angles lie in the right side of the Ramachandran plot (alpha(L) region; phi 97 degrees).
77 handed alpha-helical region (L-alpha) of the Ramachandran plot are a potential indicator of structura
78 es of amino acids in specific regions of the Ramachandran plot are preferred at the functional sites
79  many residues lie in the beta-region of the Ramachandran plot, and molecular-dynamics simulations co
80 ning the extended and helical regions of the Ramachandran plot, and they detect a predominant average
81 roline (PPII) and the helical regions of the Ramachandran plot.
82 of residues in the disallowed regions of the Ramachandran plot.
83 s possible within the allowed regions of the Ramachandran space with only minor mutations to a known
84 eta-structure, and PPII-helix regions of the Ramachandran surface and that they "flicker" between the
85 aluation of pseudotorsional space and of the Ramachandran-like eta-theta plot.
86  conformations and labeled them based on the Ramachandran regions (A, alpha; B, beta; L, left) of the
87 ued our development of methods to relate the Ramachandran Psi-angle to the amide III band frequency.
88    The obtained values are very close to the Ramachandran coordinates of the polyproline II helix (PP
89                             According to the Ramachandran plot, 77.46% of the construct's amino acid
90 formations in coil regions, that traditional Ramachandran plot outliers fall into occupied regions of
91 omenclature for all 18 beta-turn types using Ramachandran region names for the two central residues (
92 rently reporting on backbone sampling within Ramachandran substates, while a slower component (5-25 n