PubMed · 10237588
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1975. Seward minor operating table.. https://pubmed.ncbi.nlm.nih.gov/10237588/
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A theoretical and experimental investigation of the nonlinear dynamic response of a periodically excited string subject to a knife-edge amplitude restraint is presented. The amplitude restraint creates an impact condition as the amplitude of the response grows. The focus of this work is on the influence of a grazing instability; this zero-velocity impact event leads to complicated, post-bifurcation behavior ranging from multifrequency, periodic motion to chaos. In addition to looking at the response numerically, parameter combinations leading to an incidence of grazing are clearly identified in the excitation force excitation frequency parameter space using a multiple scales perturbation analysis. Modeling issues, numerical difficulties, and experimental limitations are also discussed.
We survey all the known instances of domain movements in proteins for which there is crystallographic evidence for the movement. We explain these domain movements in terms of the repertoire of low-energy conformation changes that are known to occur in proteins. We first describe the basic elements of this repertoire, hinge and shear motions, and then show how the elements of the repertoire can be combined to produce domain movements. We emphasize that the elements used in particular proteins are determined mainly by the structure of the interfaces between the domains.
Normal mode calculation is applied to tRNAPhe and tRNAAsp, and their structural and vibrational aspects are analyzed. Dihedral angles along the phosphate-ribose backbone (alpha, beta, gamma, epsilon, zeta) and dihedral angles of glycosyl bonds (chi) are selected as movable parameters. The calculated displacement of each atom agrees with experimental data. In modes with frequencies higher than 130 cm-1, the motions are localized around each stem and the elbow region of the L-shape. On the other hand, collective motions such as bending or twisting of arms are seen in modes with lower frequencies. Hinge axes and bend angles are calculated without prior knowledge. Movements in modes with very low frequencies are combinations of hinge bending motions with various hinge axes and bend angles. The thermal fluctuations of dihedral angles well reflect the structural characters of transfer RNAs. There are some dihedral angles of nucleotides located around the elbow region of L-shape, which fluctuate about five to six times more than the average value. Nucleotides in the position seem to be influential in the dynamics of the entire structure. The normal mode calculation seems to provide much information for the study of conformational changes of transfer RNAs induced by aminoacyl-tRNA synthetase or codon during molecular recognition.