Reverse turns in peptides and proteins

CRC Crit Rev Biochem. 1980;8(4):315-99. doi: 10.3109/10409238009105470.

Abstract

The evidence that reverse turns frequently occur as structural components of proteins, as well as of linear and cyclic peptides, is overwhelming. This review summarizes and examines critically the experimental evidence derived from physical methods such as 1H and 13C nuclear magnetic resonance spectroscopy, spin-lattice relaxation time, circular dichroism, IR spectroscopy, and X-ray crystallography. Secondly, theoretical evidence obtained from energy calculations, which rely on empirical energy functions, and correlative methods, which rely on algorithms based on the frequency of occurrence of amino acids, is evaluated. In particular, those theoretical studies for which complementary physical studies have been completed are emphasized. Finally, examples of structure-function relationships involving reverse turns and their biological recognition are demonstrated.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Amines
  • Anti-Bacterial Agents
  • Antitoxins
  • Chemical Phenomena
  • Chemistry, Physical
  • Circular Dichroism
  • Collagen / metabolism
  • Elastin / metabolism
  • Enkephalins
  • Glycoproteins / metabolism
  • Hormones
  • Hydrogen Bonding
  • Hydroxylation
  • Ionophores
  • Magnetic Resonance Spectroscopy
  • Muramidase / immunology
  • Peptides*
  • Phosphorylation
  • Proline / metabolism
  • Protein Conformation*
  • Proteins / immunology
  • Spectrophotometry, Infrared
  • Spectrum Analysis, Raman
  • Toxins, Biological
  • Tuftsin / analysis
  • X-Ray Diffraction

Substances

  • Amines
  • Anti-Bacterial Agents
  • Antitoxins
  • Enkephalins
  • Glycoproteins
  • Hormones
  • Ionophores
  • Peptides
  • Proteins
  • Toxins, Biological
  • Collagen
  • Elastin
  • Proline
  • Muramidase
  • Tuftsin