生物化学资料：2-protein structure.pptVIP

UNIT I Protein Structure and Function第一单元 蛋白质的结构和功能 Chapter 2 Structure of Proteins 第2章 蛋白质的结构 Cartoon representation of the Cys2His2 zinc finger motif, consisting of an α helix and an antiparallel β sheet. The zinc ion (green) is coordinated by two histidine residues and two cysteine residues IIII. TERTIARY STRUCTURE OF GLOBULAR PROTEINS Definition: the spatial arrangement of all the atoms of a protein or a subunit. (native, stable, functional structure) It refers both to the folding of domains its arrangement in the polypeptide. The primary structure of a polypeptide determines its tertiary structure. Hydrophobic side chains in the interior, hydrophilic groups on the surface of the molecule. The structure of globular proteins in aqueous solution is compact(close packing of the atoms). IV-A. Domains The basic functional 3-D structural units. Structurally functionally semi-independent Usually found in a large polypeptide. Its core is built from combinations of motifs. 纤连蛋白分子的结构域 IV-B. Interactions stabilizing tertiary structure Formation of tertiary structure depends to interactions betw. AA side chains. At least, there are 4 types of interactions for the teriary structures of globular proteins. IV-B-1. Disulfide bonds A covalent bond(-S-S-) There are inter- intra-linkage in proteins. For example, Ig IV-B-2. Hydrophobic interactions A non-covalent bond betw.2 hydrophobic AAs in the interior of soluble proteins Betw.hydrophobic AA lipid in the surface of membrane proteins IV-B-3. Hydrogen bonds A non-covalent bond AA R-chains containing –OH or –NH with O of -COO or –C=O Formation betw.polar groups on the surface of proteins . IV-B-4. Ionic bonds A non-covalent bond Betw. the counter-charged AA R-groups IV-C. Protein folding The process folding into the native conformation No need for external template. The internal residues of proteins direct its folding Driven mainly by hydrophobic forces. Through an ordered set of p