The α-helix is a common secondary structure encountered in proteins of the globular class. Within a single protein different regions of the polypeptide chain may assume different conformations determined by the primary sequence of the amino acids. It is the partial double-bond character of the peptide bond that defines the conformations a polypeptide chain may assume. Globular proteins are compactly folded and coiled, whereas, fibrous proteins are more filamentous or elongated. In general proteins fold into two broad classes of structure termed, globular proteins or fibrous proteins. These conformations constitute the secondary structures of a protein. The ordered array of amino acids in a protein confer regular conformational forms upon that protein. the end with the residue containing a free α-carboxyl group) is to the right. the end bearing the residue with the free α-amino group) is to the left (and the number 1 amino acid) and the C-terminal end (i.e. The convention for the designation of the order of amino acids is that the N-terminal end (i.e. The primary structure of peptides and proteins refers to the linear number and order of the amino acids present. High Performance Liquid Chromatography (HPLC).
Table of the Specificities of Several Exopeptidases.Carboxy-Terminal Sequence Determination.Table of the Specificities of Several Endoproteases.Analysis of Protein Structure and Composition.
0 kommentar(er)
