Conformation of biomolecules

A number of 2D NMR techniques are available for a variety of purposes They are especially valuable when attempting to determine the structure of complicated natural products and the conformations of biomolecules... 

In addition to exerting an influence on enzymatic reaction rates and the character of metabolism, temperature can also be a determining factor in the composition and conformation of biomolecules. 

Comparison of spectroscopic techniques for the determination of the solution conformation of biomolecules... 

H-N.m.r. spectroscopy has contributed significantly to extensions of our knowledge on the structure and conformation of biomolecules as well as on intra- and inter-molecular, interaction processes. N.m.r. spectroscopy is, however, an inherently insensitive technique, and the richness of information contained in an n.m.r. spectrum often limits the size and complexity of the molecules that can usefully be studied. 

Modifying the Active Conformation of Biomolecules. Class B metals such as Hg have been shown to alter the steric conformation of proteins via interactions with sulfur atoms, particularly disulphide bonds. For example, Hg insertion between the two sulfurs involved in a disulfide bond can significantly alter the shape of the protein and reduce or abolish its activity. This has been demonstrated with ribonuclease, for example. 

Altona C (1996) Vicinal Coupling Constants and Conformation of Biomolecules. In Grant DM, Harris RK (eds) Encyclopedia of Nuclear Magnetic Resonance. Wiley, New York, p 4909... 

C. Altona, Vicinal Coupling Constants and Conformation of Biomolecules. John Wiley London, 1996. 

As of the turn of the millennium, then, there had been countless sightings of CH- - -X contacts in biological systems of all sorts. And inferences had been drawn that their presence must surely influence the geometries adopted by biomolecules. But a crudal question remained open just how much do such weak H-bonds actually contribute to the conformations of biomolecules in an energetic sense Knowledge had advanced to the point that a 2001 summary [77] concluded that CH- - -O bonds constitute as much as 1/4 of all H-bonds in certain proteins so can be expected to contribute significantly to the overall... 

Cotton et al. Already in their preliminary work, the authors explored the potentialities and goals of the SERRS technique for possible applications to bioanalytical problems. The first possibility is enhanced sensitivity for the RR scattering of scarce materials. A second possibility can be added specifically to redox-active chromophores in proteins. Indeed, this new spectroelectrochemical method permits the simultaneous study of an electrochemical reaction in a biological system in conjunction with a specific measurement of subtile variations in the vibrational spectrum of the chromophores. Another striking feature of the SERRS spectroscopy is that fluorescence of the adsorbate can be completely quenched by the metal surface which generates a high-quality Raman spectrum Another common application of SERRS spectroscopy is the study of the adsorption behaviour and conformation of biomolecules at the metal/electrolyte interface. 

The NMR parameters for the determination of conformation have all been introduced in Sect. 2. To translate them into conformation of biomolecules, two protocols have survived and are applied in general. One is the dis-... 

In this section, we briefly describe our hybrid approach for predicting conformations of biomolecules stabilized in solvent [15, 16, 17]. In this approach, the RISM theory is combined with the MC simulated annealing or one of the generalized-ensemble algorithms. Our approach falls into the third category, and both the biomolecule and the solvent are treated on the atomic level. The hybrid approach is implemented for two small peptides as the first step of the research. The solvent effects on the conformational stability of the peptides are discussed and the... 

The surface chemistry of implants plays an important role in their service. During implantation, proteins and other biomolecules adsorb on the implant s surface. The changes in native conformations of biomolecules on a non physiological surface initiate a trigger cascade of inflammatory (immune) responses, which interfere with the integration of the implant into the living tissue or enhance the formation of fiber capsule. A cer-... 

Caminati, W. 2004. The rotational spectra of conformers of biomolecules Tryptamine. Phys. Chem. Chem. Phys. 6 2806-2810. 

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