Sulfur in Proteins

Sulfur in Proteins is a collection of papers presented at the 1958 Symposium on Sulfur in Proteins, held in Falmouth, Massachusetts. The symposium primary aims to explore the varied and unusual roles of –S–S– and –SH groups in proteins.
This book is organized into eight chapters that cover a wide variety of proteins, including serum, iron, copper, and muscle proteins, as well as enzymes and viruses. The opening chapter describes the various protein reactions involving sulfur, emphasizing the chemical modification of thiol and disulfide groups. Considerable chapters are devoted to the chemical properties, biogenesis, reactivity, and oxygenation of specific proteins. A chapter highlights some aspects of protein structure in relation to the role of –S–S– and –SH groups in enzymic catalysis. This chapter also describes the properties of sulfhydryl groups in yeast alcohol dehydrogenase. The final chapters examine the role of sulfur groups in several virus proteins and in cell division. This work will be of great value to protein scientists and researchers.

Participants Introduction I. Protein Reactions Involving Sulfur I.1. Chemical Modification of Thiol and Disulfide Groups in Proteins and Peptides I.2. The Introduction of New Sulfhydryl Groups and Disulfide Bonds into Proteins I.3. Disulfide Bonds in Proteins I.4. The Varying Reactivity of the Cystine of Wool I.5. A High-Sulfur Protein from Wool I.6. The Decomposition of Keratin by Microorganisms I.7. The Supercontraction of Keratin Fibers by Lithium Bromide II. Serum Proteins II.1. Some Chemical Properties of the Sulfhydryl Group in Bovine Plasma Albumin II.2. Relative Probabilities of Isomers in Cystine-Containing Randomly Coiled Polypeptides II.3. Biogenesis of Protein Fibers: The Clotting of Blood Plasma III. Iron and Copper Proteins III.1. The Role of Sulfur in Some Metal-Proteins III.2. The Role of Sulfur in Cytochrome c III.3. The Cystine/Cysteine Content of Hemoglobins III.4. Sulfhydryl Groups and the Oxygenation of Hemoglobin III.5. Relation of Iron to Sulfhydryl Groups in Ferritin IV. Enzymes IV.1. Some Aspects of Protein Structure in Relation to the Role of —SH and —S—S— Groups in Enzymic Catalysis IV.2. Mechanism of Action of Alcohol Dehydrogenases from Yeast and Liver and β-Galactosidase of E. coli IV.3. Determination and Properties of Sulfhydryl Groups in Yeast Alcohol Dehydrogenase IV.4. Fluorometric Analysis of Coenzyme Binding and Thiol Interactions on Glyceraldehyde-3-phosphate and Lactic Dehydrogenases IV.5. On the Order of Disulfide Bond Reduction in Ribonuclease V. Muscle Proteins V.l. Cysteine and Cystine Content of Muscle Protein Fractions V.2. The Role of SH Groups in the Interaction of Myosin with Phosphate Compounds and with Actin V.3. Studies on the Functional Sulfhydryl Groups of Myosin and Actin VI. Viruses VI.l. The Masked —SH Group in Tobacco Mosaic Virus Protein VI.2. Structure an