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Cell Physiology Sourcebook, Third Edition: A Molecular by Nicholas Sperelakis PDF

By Nicholas Sperelakis

ISBN-10: 0126569762

ISBN-13: 9780126569766

This thoroughly revised and up-to-date resource booklet presents finished and authoritative assurance of mobile body structure and membrane biophysics. meant essentially as a textual content for complicated undergraduate and graduate scholars and as a reference for researchers, this multidisciplinary e-book comprises a number of new chapters and is a useful reduction to scientists drawn to cellphone body structure, biophysics, phone biology, electrophysiology, and cellphone signaling.

* comprises wide assurance of either animal and plant cells
* Appendices overview fundamentals of the propagation of motion potentials, electrical energy, and cable homes

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Nicholas Sperelakis's Cell Physiology Sourcebook, Third Edition: A Molecular PDF

This thoroughly revised and up to date resource booklet offers entire and authoritative assurance of phone body structure and membrane biophysics. meant basically as a textual content for complex undergraduate and graduate scholars and as a reference for researchers, this multidisciplinary ebook contains a number of new chapters and is a useful relief to scientists attracted to mobile body structure, biophysics, cellphone biology, electrophysiology, and mobile signaling.

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Additional info for Cell Physiology Sourcebook, Third Edition: A Molecular Approach

Example text

These calculations have thus far been aimed at determination of the intrinsic PKaS of specific groups on protein surfaces. In this approach (Russell and Warshel, 1985), the energy of dissociation of a particular acid group, AH, is computed for the whole protein surrounded by water molecules placed on a grid around the protein. D. Included in this energy is the effect of the permanent dipoles of the atoms of the protein that induce dipoles on the other atoms of the protein. The magnitude of this energy depends on the polarizability of the interacting atoms.

If we wish to identify a particular protein on an electrophoretogram, we can use a "tagged" antibody to the protein and reveal its presence on the electrophoretic gel. The antibody is "tagged" with a covalently labeled enzyme that catalyzes a reaction that produces a chromophoric (colored) reaction product. For example, alkaline phosphatase catalyzes the hydrolysis of p-nitrophenol phosphate, which is colorless, to p-nitrophenol, which is bright yellow. Since antibody cannot be added directly to the gel from electrophoresis, the gel itself is blotted onto nitrocellulose or another suitable membrane that contains all of the separated bands of proteins as they were on the original electrophoretic gel.

Evidently, other interactions are important in stabilizing/3sheets besides backbone-backbone hydrogen bonding. Another type of regular structure is the reverse turn, the prototype of which is shown in Fig. 3C. In this structure, the polypeptide chain reverses its direction. A minimum of two amino acids is needed to form a reverse or hairpin turn, which is also called a 0-bend. Usually three amino acids are involved, however, because the C=O of the first residue can form an i-to-i+3 hydrogen bond with the N - H of the i+3rd residue, as shown in Fig.

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Cell Physiology Sourcebook, Third Edition: A Molecular Approach by Nicholas Sperelakis


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