Coupling of Phosphorylation to Electron and Hydrogen Transfer by a Chemi-Osmotic type of Mechanism

1Scientists these days tend to keep up a polite fiction that all science is equal. Except for the work of the misguided opponent whose arguments we happen to be refuting at the time, we speak as though every scientist's field and methods of study are as good as every other scientist's and perhaps a little better. This keeps us all cordial when it comes to recommending each other for government grants. But I think anyone who looks at the matter closely will agree that some fields of science are moving forward very much faster than others, perhaps by an order of magnitude, if numbers could be put on such estimates. The discoveries leap from the headlines - and they are real advances in complex and difficult subjects, like molecular biology and highenergy physics. As Alvin Weinberg says (1) "Hardly a month goes by without a stunning success in molecular biology being reported in the Proceedings of the National Academy of Sciences."

http://www.bio.miami.edu/dana/dox/Platt_1964.pdf

Certain systematic methods of scientific thinking may produce much more rapid progress than others.

Publisher Summary This chapter reviews that the simplest way of accounting for the absorption spectrum of a protein is as the sum of the spectra of its components. This gives results which are often good approximations to the observed protein spectrum. The assumption of additivity is basic for useful analytical applications of spectral measurements. It discusses that in another perspective, the failure of perfect additivity of the component absorptivities affords the possibility of obtaining structural information about proteins. The absorptivity of the peptide bond can change by as much as a factor of two with a change in the conformation of a peptide chain. Since the absorptivity of aromatic side chains is much less sensitive to environmental change, correspondingly, more sensitive techniques are required to measure the small changes which do occur. The nature and limitations of the structural information resulting from both peptide-bond and side-chain absorption are discussed. Absorption spectra can occasionally be a useful tool in the identification of unusual structural features in proteins and polypeptides. Several such applications are also explained in this chapter.

Ultraviolet spectra Of Proteins and Amino Acids

http://www.chem.ualberta.ca/~campbell/resources/Bioanalytical-2012/Ribosome_Steitz_short.pdf

RNA, the first macromolecular catalyst: the ribosome is a ribozyme

The assumption of locally additive forces is used to describe the London—van der Waals dispersion attraction between long saturated chains. For two linear chains of length L, opposed and parallel, each built out of N identical units of length λ(Nλ=L), the total dispersion energy is given by W=A4λ2D4ρ(3tan−1ρ+ρ1+ρ2),  ρ=LD, where D is the mutual distance of the two chains; A is the coefficient of the dispersion interaction between two basic units. At distances D much smaller than the molecular length L, the energy becomes proportional to L (or N) and inversely proportional to the fifth power of the intermolecular distance.The coefficient A is calculated for the interaction between two CH2 units in hydrocarbon chains and the result is used to estimate the sublimation energy at 0°K of paraffin crystals. Sound agreement with experiment is obtained. Finally, the particularities of the attractive forces between long saturated chains are examined in more detail and their great sensitivity to distance is shown by...

R. H. Bolt

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Biophysical Science-A Study Program

Biophysical science???a study program

Biophysical Science; A Study Program