Showing papers in "Advances in Protein Chemistry in 1968"
TL;DR: This chapter considers the parameters that are required for an adequate description of a polypeptide chain and the mathematical method of utilizing these parameters for calculating the coordinates of all the atoms in a suitable frame of reference so that all the interatomic distances, and bond angles, can be calculated and their consequences worked out.
Abstract: Publisher Summary This chapter deals with the recent developments regarding the description and nature of the conformation of proteins and polypeptides with special reference to the stereochemical aspects of the problem. This chapter considers the parameters that are required for an adequate description of a polypeptide chain. This chapter focuses the attention on what may be called “internal parameters”—that is, those which can be defined in terms of the relationships among atoms or units that form the building blocks of the polypeptide chains. This chapter also provides an account of the mathematical method of utilizing these parameters for calculating the coordinates of all the atoms in a suitable frame of reference, so that all the interatomic distances, and bond angles, can be calculated and their consequences worked out. This chapter observes conformations in amino acids, peptides, polypeptides, and proteins.
2,802 citations
TL;DR: This chapter illustrates that the underlying principle of all relaxation techniques is similar—namely, by rapidly changing some external parameter the thermodynamic state of the system is changed and kinetic studies are made by measurement of the rate of change of concentrations as they approach the new thermodynamics state.
Abstract: Publisher Summary This chapter discusses relaxation spectrometry of biological systems. The introduction of relaxation techniques as methods for studying chemical kinetics in liquid solutions took place in early times. Since then the use of relaxation methods has produced exciting new results in many different areas of chemistry. This chapter illustrates that the underlying principle of all relaxation techniques is similar—namely, by rapidly changing some external parameter (e.g., temperature or pressure) the thermodynamic state of the system is changed— kinetic studies are made by measurement of the rate of change of concentrations as they approach the new thermodynamic state. Moreover many reactions of biological interest (e.g., enzymatic reactions) are quite rapid; therefore, this feature of relaxation methods is of importance in the study of mechanisms of biological reactions. This chapter discusses the principles and experimental techniques involved in relaxation spectrometry. The chapter also addresses experimental techniques. This chapter concludes by discussing specific studies of the relaxation spectra of biochemical or closely related systems.
146 citations
TL;DR: This chapter explores that it is necessary to include a brief theoretical outline of the fundamental problem of protein crystallography and the method currently used in its solution, the practical aspects are the main concerns of this chapter.
Abstract: Publisher Summary This chapter discusses the preparation of isomorphous derivatives, which represents the main-research effort in protein structure laboratories at the present time The chemical problem of combining compounds that contain atoms of high atomic number with crystalline proteins to form suitable derivatives is made more difficult by severely restrictive crystallographic criterion, if isomorphism must be satisfied However, the applications of isomorphous replacement to fully determined protein structures shows great promise in the determination of protein function and more particularly enzyme function This chapter explores that it is necessary to include a brief theoretical outline of the fundamental problem of protein crystallography and the method currently used in its solution, the practical aspects are the main concerns of this chapter
42 citations