Titlebook: NMR of Biological Macromolecules; Chariklia Ioannidou Stassinopoulou Conference proceedings 1994 Springer-Verlag Berlin Heidelberg 1994 Bi

變化

小官

Principles of Multidimensional NMR, solve structures of small proteins or nucleic acids in solution. Thus, NMR has evolved from an esoteric technique to a major analytical tool. NMR experiments are built from a combination of various radio frequency pulses separated by delays, and the oscillation of the radiofrequency of the pulses m

Ligament

小卒

Computer-Assisted Structure Determination of Biomacromolecules by NMR,d 100 amino acids (Wagner 1993). The resulting growth in complexity of the NMR spectra places an increasingly important role on computer programs that support the interpretation of the spectra and the management of the assignment data. When the earliest NMR structure determinations were accomplished

habitat

Nuclear Shielding and Biomolecular Structure,es, they are subject to the laws of electromagnetic induction. The net effect of the magnetic field is to superimpose a motion of electrons around the field axis on the orbital motion of the electron. In addition, the applied field will polarize the electron cloud. The motion of the electron generat

休戰(zhàn)

Breach

NMR Studies of Ligand-Protein Interactions Involving Quadrupolar Nuclei, possess nuclear quadrupole moments which shorten relaxation times and broaden lines. This renders the nuclei less suitable, in general, for biological NMR applications than nuclei with I=?. During the last decade or so there has, however, been considerable methodological progress in this particular

桉樹

septicemia

Insubordinate

Long Time Protein Dynamics,on diffuses in a complex conformational energy landscape with a large number of energy valleys separated by energy barriers (Young et al. 1991). Local dynamics in polypeptides, as described by NMR relaxation or fluorescence anisotropy, are very sensitive to the structure of the residues, to the inte