title: Zinc-dependent protein folding.
abstract: Studies of classic zinc-finger peptides over the past 15 years have offered insights into the coupled processes of metal binding and protein folding. Within the past two years, this insight has been used to increase our understanding of the importance of first and second shell contributions (i.e. contributions from direct and indirect metal ligands) to metal binding and protein-folding stability, and led to advances in de novo protein design and protein redesign.
authors.affiliation: Center for Environmental Bioinorganic Chemistry, Department of Geosciences, Princeton University, Princeton, 08544, USA. ehcox@princeton.edu
authors.forename: E H
authors.initials: EH
authors.lastname: Cox
authors.forename: G L
authors.initials: GL
authors.lastname: McLendon
mesh_terms: D000595:Amino Acid Sequence; D008969:Molecular Sequence Data; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D013816:Thermodynamics; D015032:Zinc / Q000378:metabolism*; D016335:Zinc Fingers
chemical_list: D011506:Proteins; D015032:Zinc