Design of beta-sheet systems for understanding the thermodynamics and kinetics of protein folding.
Peptide beta-sheet systems have emerged as context-independent models for probing secondary structure propensities, the nature and magnitude of stabilizing weak interactions, and aspects of cooperativity both parallel and perpendicular to the strand direction. These systems have allowed fundamental advances in understanding non-covalent interactions relevant to both chemical and biological systems, and in describing the protein folding energy landscape.
School of Chemistry, Centre for Biomolecular Sciences, University Park, Nottingham NG7 2RD, UK. mark.searle@nottingham.ac.uk
Mark S
MS
Searle
Barbara
B
Ciani
D007700:Kinetics; D008958:Models, Molecular; D015202:Protein Engineering; D017510:Protein Folding; D017433:Protein Structure, Secondary; D013329:Structure-Activity Relationship; D013816:Thermodynamics; D025801:Ubiquitin / Q000737:chemistry
D025801:Ubiquitin