By Robert K. Murray, Darryl K. Granner, Peter A. Mayes, Victor W. Rodwell
Harper's Illustrated Biochemistry deals concise, up to date, and authoritative assurance of the foundations of biochemistry and molecular biology as they relate to medicine.
* Revised for readability, with new streamlined association, new figures, and new on-line snapshot assortment * displays significant advances in biochemistry which are vital to drugs * contains new chapters on amino acids and peptides, fundamental constitution of proteins, and the Human Genome venture * offers new and improved insurance of the mechanisms of motion of enzymes, receptors curious about lipoprotein metabolism and opposite ldl cholesterol shipping, RNA synthesis, gene law, molecular mechanisms of hormone motion, protein existence cycle, and pharmacogenomics * presents medical correlations and bankruptcy summaries * good points greater than 500 transparent, descriptive illustrations
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However, disulfide bond formation is nonspecific. Under oxidizing conditions, a given cysteine can form a disulfide bond with the SH of any accessible cysteinyl residue. By catalyzing disulfide exchange, the rupture of an SS bond and its reformation with a different partner cysteine, protein disulfide isomerase facilitates the formation of disulfide bonds that stabilize their native conformation. Proline-cis,trans-Isomerase All X-Pro peptide bonds—where X represents any residue—are synthesized in the trans configuration.
The hydrogen-donating α-nitrogen atoms are shown as blue circles. Hydrogen bonds are indicated by dotted lines. For clarity in presentation, R groups and hydrogens are omitted. Top: Antiparallel β sheet. Pairs of hydrogen bonds alternate between being close together and wide apart and are oriented approximately perpendicular to the polypeptide backbone. Bottom: Parallel β sheet. The hydrogen bonds are evenly spaced but slant in alternate directions. dered regions assume an ordered conformation upon binding of a ligand.
Chaperones prevent aggregation, thus providing an opportunity for the formation of appropriate secondary structural elements and their subsequent coalescence into a molten globule. The hsp60 family of chaperones, sometimes called chaperonins, differ in sequence and structure from hsp70 and its homologs. Hsp60 acts later in the folding process, often together with an hsp70 chaperone. qxd 2/13/2003 2:06 PM Page 37 PROTEINS: HIGHER ORDERS OF STRUCTURE shaped hsp60 chaperone provides a sheltered environment in which a polypeptide can fold until all hydrophobic regions are buried in its interior, eliminating aggregation.