By John N. Abelson, Melvin I. Simon, Gary K. Ackers, Michael L. Johnson

General Description of the Volume:
The very lifestyles of organic constructions and their sensible interactions are dictated through full of life relationships. hence the critical topic of this quantity is that thermodynamic tools, i.e. options that probe the energetics of organic macromolecules, now contain a robust and sensible relatives of instruments for study in glossy biology. the appliance of thermodynamics and statistical thermodynamics to biochemical and biophysical structures is gifted. This quantity supplementations Methods in Enzymology, quantity 259.
General Description of the Series:
The seriously acclaimed laboratory usual for greater than 40 years, Methods in Enzymology is likely one of the such a lot hugely revered guides within the box of biochemistry. seeing that 1955, every one quantity has been eagerly awaited, usually consulted, and praised via researchers and reviewers alike. Now with greater than three hundred volumes (all of them nonetheless in print), the sequence comprises a lot fabric nonetheless appropriate today--truly a vital ebook for researchers in all fields of existence sciences.

Key Features
* significant themes coated include:
* interpreting ideas of helix balance in peptides
* Protein Folding in Membranes
* Molecular Crowding
* research of the Bohr impression in Hemoglobin Intermediates
* Photoacoustic Calorimetry of Proteins
* Theoretical facets of Isothermal Titration Calorimetry
* lively tips on how to research Bifunctional Biotin Repressor

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Additional resources for Energetics of Biological Macromolecules Part B

Sample text

This procedure returns the w value in the Lifson-Roig notation for the new side chain, without fitting the enthalpy or any other property of the residue, such as side chain-side chain interactions.

AMINO ACIDS AS PROBES OF HELIX STABILITY 27 and the associated thermodynamic parameters. A complete description of these parameters could improve algorithms for predicting protein structure from primary amino acid sequence data. 4'5 One fundamental problem that needs to be addressed is whether it is useful to speak of intrinsic c~ helix, turn, or/3 sheet forming tendencies or "propensities" for each amino acid. It is tempting to suppose that a given side chain can be associated with a free energy that reflects specific interactions between that side chain and the peptide backbone in the c~ helix or/~-sheet conformation.

Consequently it is desirable to keep the mean helix contents of both test and reference peptides within this range. The mean helix content of peptides is most easily modulated by varying the peptide chain length because the helix content increases with chain length for peptides of similar composition and sequence. Limitations of the experimental method for determining helix content must also be taken into account. Although circular dichroism measures the absolute value offH with equal sensitivity throughout the whole transition, error resulting from baseline uncertainty is minimal for peptides that have mean helix contents near 50% (see earlier).

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