scispace - formally typeset
Journal ArticleDOI

Proteins, Amino-Acids and Peptides as Ions and Dipolar Ions

Kenneth C. Bailey
- 06 Oct 1945 - 
- Vol. 156, Iss: 3962, pp 405-406
TLDR
Cohn and Cohn as discussed by the authors published Proteins, Amino-Acids and Peptides as Ions and Dipolar Ions, with chapters by John G. Kirkwood, Hans Mueller, J. L. Oncley and George Scatchard.
Abstract
THE misfortunes of war have rendered this impressive book, published in 1943, inaccessible in Britain until recent months. No shorter description is possible than to say it is worthy of those great men to whom it is dedicated, Bate Hardy, Loeb, Osborne and Sorensen. Proteins, Amino-Acids and Peptides as Ions and Dipolar Ions Edwin J. Cohn John T. Edsall, with chapters by John G. Kirkwood, Hans Mueller, J. L. Oncley and George Scatchard. Pp. xviii + 686. American Chemical Society Monograph Series. (New York: Reinhold Publishing Corporation, 1943.) 13.50 dollars.

read more

Citations
More filters
Journal ArticleDOI

A Continuum of Anionic Charge: Structures and Functions of d-Alanyl-Teichoic Acids in Gram-Positive Bacteria

TL;DR: The structures and functions of d- alanyl-TAs, the d-alanylation system encoded by the dlt operon, and the roles of TAs in cell growth are addressed.
Journal ArticleDOI

A molecular mechanism for osmolyte-induced protein stability

TL;DR: A quantitative solvation model is constructed in which backbone/solvent interaction energy is a function of interactant polarity, and the number of energetically equivalent ways of realizing a given interaction is afunction of interactionant surface area.
Journal ArticleDOI

Volume changes on protein folding.

TL;DR: The exceptionally high density of the protein interior shown here implies that packing forces play a more important role in protein stability than has been believed hitherto.
Journal ArticleDOI

The packing density in proteins: standard radii and volumes.

TL;DR: This analysis shows that, if the surface water molecules are included in the calculations, the overall packing efficiency throughout the protein interior is high and fairly uniform, but if the water structure is removed, the packing efficiency in peripheral regions of theprotein interior is underestimated.
Journal ArticleDOI

Electrostatic Interactions in Protein Structure, Folding, Binding, and Condensation

TL;DR: This review will examine how charged side chains are spatially distributed in various types of proteins and how electrostatic interactions affect thermodynamic and kinetic properties of proteins.
References
More filters
Journal ArticleDOI

A Continuum of Anionic Charge: Structures and Functions of d-Alanyl-Teichoic Acids in Gram-Positive Bacteria

TL;DR: The structures and functions of d- alanyl-TAs, the d-alanylation system encoded by the dlt operon, and the roles of TAs in cell growth are addressed.
Journal ArticleDOI

A molecular mechanism for osmolyte-induced protein stability

TL;DR: A quantitative solvation model is constructed in which backbone/solvent interaction energy is a function of interactant polarity, and the number of energetically equivalent ways of realizing a given interaction is afunction of interactionant surface area.
Journal ArticleDOI

Volume changes on protein folding.

TL;DR: The exceptionally high density of the protein interior shown here implies that packing forces play a more important role in protein stability than has been believed hitherto.
Journal ArticleDOI

Electrostatic Interactions in Protein Structure, Folding, Binding, and Condensation

TL;DR: This review will examine how charged side chains are spatially distributed in various types of proteins and how electrostatic interactions affect thermodynamic and kinetic properties of proteins.
Journal ArticleDOI

Predicting the energetics of osmolyte-induced protein folding/unfolding

TL;DR: It is demonstrated that the long-sought goal of predicting solvent-dependent cooperative protein folding/unfolding free-energy changes (m values) can be achieved and the approach permits dissection of the folding/uns folding free- energy changes into individual contributions from the peptide backbone and residue side chains.