The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis

Poly(N-isopropylacrylamide): experiment, theory and application

The Regulation of Rabbit Skeletal Muscle Contraction I. BIOCHEMICAL STUDIES OF THE INTERACTION OF THE TROPOMYOSIN-TROPONIN COMPLEX WITH ACTIN AND THE PROTEOLYTIC FRAGMENTS OF MYOSIN

T e purpose of this review is to assess the nature and magnitudes of the dominant forces in protein folding. Since proteins are only marginally stable at room temperature,’ no type of molecular interaction is unimportant, and even small interactions can contribute significantly (positively or negatively) to stability (Alber, 1989a,b; Matthews, 1987a,b). However, the present review aims to identify only the largest forces that lead to the structural features of globular proteins: their extraordinary compactness, their core of nonpolar residues, and their considerable amounts of internal architecture. This review explores contributions to the free energy of folding arising from electrostatics (classical charge repulsions and ion pairing), hydrogen-bonding and van der Waals interactions, intrinsic propensities, and hydrophobic interactions. An earlier review by Kauzmann (1959) introduced the importance of hydrophobic interactions. His insights were particularly remarkable considering that he did not have the benefit of known protein structures, model studies, high-resolution calorimetry, mutational methods, or force-field or statistical mechanical results. The present review aims to provide a reassessment of the factors important for folding in light of current knowledge. Also considered here are the opposing forces, conformational entropy and electrostatics. The process of protein folding has been known for about 60 years. In 1902, Emil Fischer and Franz Hofmeister independently concluded that proteins were chains of covalently linked amino acids (Haschemeyer & Haschemeyer, 1973) but deeper understanding of protein structure and conformational change was hindered because of the difficulty in finding conditions for solubilization. Chick and Martin (191 1) were the first to discover the process of denaturation and to distinguish it from the process of aggregation. By 1925, the denaturation process was considered to be either hydrolysis of the peptide bond (Wu & Wu, 1925; Anson & Mirsky, 1925) or dehydration of the protein (Robertson, 1918). The view that protein denaturation was an unfolding process was

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Dominant forces in protein folding

The helix, s Applequist, 1963) in which the Zimm-Bragg parameters u and s are defined respectively as the cooperativity factor for helix initiation, and the equi- librium constant for converting a coil residue to a helical ~~~~

Conformational parameters for amino acids in helical, beta-sheet, and random coil regions calculated from proteins.

Polypeptides. IV. The Molecular Weight, Configuration and Association of Poly-γ-benzyl-L-glutamate in Various Solvents

The hydrophobic bond in micellar systems. Effects of various additives on the stability of micelles of sodium dodecyl sulfate and of n-dodecyltrimethylammonium bromide.

Alfred Holtzer

Papers

Polypeptides. IV. The Molecular Weight, Configuration and Association of Poly-γ-benzyl-L-glutamate in Various Solvents

The hydrophobic bond in micellar systems. Effects of various additives on the stability of micelles of sodium dodecyl sulfate and of n-dodecyltrimethylammonium bromide.

The Helix-Coil Transition in Solutions of Polyglutamic Acid

On the ionic strength dependence of micelle number. II.

The Molecular Weight, Size and Shape of the Myosin Molecule