Structure and dynamics in proteins of pharmacological interest.
This paper begins with a brief survey of the standard nuclear magnetic resonance (NMR) method for protein structure determination in solution, which has been applied successfully with numerous globular proteins with molecular weights in the range from 3,000 to 15,000. The results obtained show that for the core of globular proteins, the quality of the structures determined in solution can be comparable to that achieved with diffraction techniques using protein single crystals. In addition, they also indicate that a complete description of proteins in solution may include short-lived, transient structural features that could be of crucial importance for the functional properties. Several supplementary NMR techniques capable of characterizing diverse aspects of flexible polypeptide chains are discussed.
Wüthrich
K
K
Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule-Hönggerberg, Zürich, Switzerland.
D000595:Amino Acid Sequence; D006860:Hydrogen Bonding; D006863:Hydrogen-Ion Concentration; D007930:Leucine; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008969:Molecular Sequence Data; D010455:Peptides; D011487:Protein Conformation; D011506:Proteins / Q000378:metabolism; D012996:Solutions; D014633:Valine
D010455:Peptides; D011506:Proteins; D012996:Solutions; D007930:Leucine; D014633:Valine