Biophysics methods section

Cross-linking constrains the conformational flexibility of biopolymers and, as a rule, stabilizes their secondary, tertiary, and quaternary structures against the denaturing effects of high temperatures.29 We used differential scanning calorimetry (DSC) to compare the heat-induced conformational transitions of selected RNase A samples that were characterized in Figure 15.2. A brief introduction to DSC is provided in Section 15.15.1 for those readers unfamiliar with this biophysical method. Trace 1 in Figure 15.3a is the heat absorption... 

The effect of formalin-treatment on the structural properties of RNase A was examined using circular dichroism (CD) spectropolarimetry. A brief introduction to CD spectropolarimetry is provided in Section 15.15.2 for those readers unfamiliar with this biophysical method. The secondary structure of RNase A consists of one long four-stranded anti-parallel p-sheet and three short a-helixes,44 which places RNase A in the a + p structural class of proteins. The effect of a 9-day incubation of RNase A (6.5mg/mL) in 10% formalin on the protein secondary structure was examined with CD spectropolarimetry in the far-UV region (170-240nm) as shown in Figure 15.6a. The resulting... 

In Sections II and III, the crystal structure of rhodopsin is briefly reviewed and compared with the dynamic structure in micellar solutions and membranes as inferred from the biophysical methods mentioned above. A structural model of the cytoplasmic surface derived from solution NMR of peptides has been presented (Ifeagle et al., 1997 Katagadda et al., 2001), but this approach does not provide direct information on... 

Monte Carlo search methods are stochastic techniques based on the use of random numbers and probability statistics to sample conformational space. The name Monte Carlo was originally coined by Metropolis and Ulam [4] during the Manhattan Project of World War II because of the similarity of this simulation technique to games of chance. Today a variety of Monte Carlo (MC) simulation methods are routinely used in diverse fields such as atmospheric studies, nuclear physics, traffic flow, and, of course, biochemistry and biophysics. In this section we focus on the application of the Monte Carlo method for... 

Biophysical constructs which have been adduced are sketched in Sections 3.1 and 3.2, and an analysis of the coupling between external EM fields and those subsystems not tractable by the methods of Section 2 is presented in Sections 3.3 and 3.4. 

Each of the individual chapters in this volume presents references to authoritative monographs or compendia of relevant information on the main topic covered. There are, in addition, introductory books that describe a broad range of relevant methods these books are particularly helpful in making the initial decision as to which spectroscopic methods to choose for a particular problem. Sections that involve spectroscopy are included in a variety of texts in biochemistry, physical chemistry for biological scientists,or biophysics. At a somewhat more advanced... 

Protein required for wool and meat based on the methods of CSIRO (2007) and following the protocols of LEAP (2014a) and Wiedemann et al. (2015) for biophysical allocation from sheep (the base case) as described in Section 10.2.3... 

Ihe Mossbauer effect Is based on the resonant absorption of nuclear gamma radiations certain stable nuclear Isotopes. Discovered by Rudolph Mossbauer in 1957, the i enmnenmi spawned a technique which has since had numerous applications in biophysics. With the exception of T e, which is about 2.2% in abundance in the natural isotopic mixtvire of iron, none of the other Mossbauer isotopes occur in high proportion in biomolecules. However, some of these isotopes may be introduced into biological macromolecules by the so called enrichment methods. Mossbauer isotopes most often used for biological applications are T e, and I. It is not possible to present a complete analysis of this phenomenon in this section a brief explanation and a brief idea about the applications of this technique is given below. 

Biophysics offers a variety of accurate methods that enable kinetic resolution in the submillisecond time scale as well as high protein structural resolution. This section summarizes some of the most frequently used techniques for the biophysical analysis of proteins. 

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