Energetics of Biological Macromolecules Part B - download pdf or read online

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

ISBN-10: 0076687929

ISBN-13: 9780076687923

ISBN-10: 012182196X

ISBN-13: 9780121821968

General Description of the Volume:
The very life of organic constructions and their sensible interactions are dictated by means of full of life relationships. hence the principal subject of this quantity is that thermodynamic equipment, i.e. innovations that probe the energetics of organic macromolecules, now contain a robust and sensible family members of instruments for study in sleek biology. the applying of thermodynamics and statistical thermodynamics to biochemical and biophysical platforms is gifted. This quantity vitamins Methods in Enzymology, quantity 259.
General Description of the Series:
The severely acclaimed laboratory ordinary for greater than 40 years, Methods in Enzymology is without doubt one of the such a lot hugely revered guides within the box of biochemistry. for the reason that 1955, every one quantity has been eagerly awaited, usually consulted, and praised by way of researchers and reviewers alike. Now with greater than three hundred volumes (all of them nonetheless in print), the sequence includes a lot fabric nonetheless suitable today--truly a necessary e-book for researchers in all fields of lifestyles sciences.

Key Features
* significant themes coated include:
* decoding principles of helix balance in peptides
* Protein Folding in Membranes
* Molecular Crowding
* examine of the Bohr impression in Hemoglobin Intermediates
* Photoacoustic Calorimetry of Proteins
* Theoretical points of Isothermal Titration Calorimetry
* full of life how to examine Bifunctional Biotin Repressor

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Extra resources for Energetics of Biological Macromolecules Part B

Example text

E. Wemmer, N. R. Kallenbach, L. Mayne, Y. Bai, and S. W. Englander, J. Am. Chem. Soc. 116, 1139 (1994). 39 H. Qian and S. I. Chan, J. Mol. Biol. 261, 279 (1996). 26 ENERGETICS OF BIOLOGICAL MACROMOLECULES [2] helix stability by methods such as those discussed here will complete the parameterization of the helix model and should allow the prediction of helix content as a final test of our understanding of the rules of helix stability. [21 Modified Amino Acids as Probes of Helix Stability By N E V I L L E R.

At a specific position in the peptide chain, changes in some of the helix parameters will have a greater effect on the calculated helix content than variation in other parameters. For example, the N-cap parameter of an amino acid makes the largest difference in the mean helix content when that amino acid occupies the first position in an unblocked peptide because the first unit in a peptide chain can only be either at the N-cap position of a helix or part of a random coil. At internal positions in the peptide, capping effects are generally overwhelmed by the propagation propensities because internal residues are more likely to be embedded in a helical segment than at the cap position.

A second approximation pointed out by Shalongo and Stellwagen 1° is the use of a linear model to describe a statistical population. Because a helical peptide populates an ensemble of conformations containing helical segments of differing lengths and, consequently, differing end effects, the linear relationship between mean helix content and ellipticity given in Eq. (6) is not strictly correct. Direct comparison of the predictions of a statistical mechanical treatment of the dichroism and the simple linear model demonstrates, however, that the error introduced by the linear approximation is insignificant as long as the baseline parameters and chain-length correction parameter are held 12j.

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Energetics of Biological Macromolecules Part B by John N. Abelson, Melvin I. Simon, Gary K. Ackers, Michael L. Johnson

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