The Configurational Changes of Poly-L-proline in Solution
01 Oct 1960-Journal of the American Chemical Society (American Chemical Society)-Vol. 82, Iss: 20, pp 5263-5279
About: This article is published in Journal of the American Chemical Society.The article was published on 1960-10-01. It has received 241 citations till now. The article focuses on the topics: Proline.
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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.
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1,167 citations
01 Jun 1963
443 citations
TL;DR: An extension of the spectral range of measurement toward optically active absorption bands in the far ultraviolet is expected to yield new information about the rotatory power of the peptide bond and thus enhance the interaction of theory and observation that has already proved fruitful.
Abstract: Publisher Summary This chapter focuses on the capacity of the optical rotatory methods to discern mixtures of this conformation with disordered regions. It discusses the manner in which theoretical considerations have provided the forms into which rotatory data are currently cast, the calibration of their constants by studies of synthetic polypeptides in known conformation, and then, the application of these equations and scales in the structural interpretation of the rotatory dispersion of proteins. This pattern of analysis undergoes refinement and revision as these methods are applied to new species of polypeptide and protein in concert with other means of conformational assignment. An extension of the spectral range of measurement toward optically active absorption bands in the far ultraviolet is expected to yield new information about the rotatory power of the peptide bond and thus enhance the interaction of theory and observation that has already proved fruitful.
373 citations
TL;DR: This chapter reviews that collagen constitutes the major protein component of skin, bone, tendon, and all the other forms of connective tissue and that the collagen ⇆ gelatin transformation in solution has been recognized as a reversible first-order phase transition, subject to the same physical laws which govern the crystalline ⇆ amorphous phase transitions observed in systems of linear polymers.
Abstract: Publisher Summary This chapter reviews that collagen constitutes the major protein component of skin, bone, tendon, and all the other forms of connective tissue. An understanding of collagen seems to the clinician to be a necessary prerequisite to a rational attack on many and diverse connective tissue disorders currently lumped together as “collagen diseases.” The unusual amino acid composition of collagen had also been recognized for some time. One-third of the residues of all collagens seemed to be glycine, while about one-fourth were proline and hydroxyproline. However, the stereochemical consequences of the presence of these residues has only become clear as a result of the detailed studies of synthetic homo- and copolymers of glycine and proline. Consideration of such synthetic polypeptides as simplified models of certain features of collagen and gelatin has been extremely helpful in recent years, and constitutes the rationale for the inclusion of a section dealing specifically with these synthetic polypeptides in this chapter. It also reviews that the collagen ⇆ gelatin transformation in solution has been recognized as a reversible first-order phase transition, subject to the same physical laws which govern the crystalline ⇆ amorphous phase transitions observed in systems of linear polymers. The direct relationship between the transition in solution and the well-known thermal shrinkage phenomenon exhibited by collagen fibers has also been established.
349 citations