title: Understanding how small helical proteins fold: conformational dynamics of Im proteins relevant to their folding landscapes.
abstract: Understanding the mechanism of folding of small proteins requires characterization of their starting unfolded states and any partially unfolded states populated during folding. Here, we review what is known from NMR about these states of Im7, a 4-helix bundle protein that folds via an on-pathway intermediate, and show that there is an alignment of non-native structure in urea-unfolded Im7 with the helices of native Im7 that is a consequence of hydrophobic helix-promoting residues also promoting cluster-formation in the unfolded protein. We suggest that this kind of alignment is present in other proteins and is relevant to how native state topology determines folding rates.
authors.affiliation: Centre for Molecular and Structural Biochemistry, School of Chemistry, University of East Anglia, Norwich NR4 7TJ, U.K.
authors.forename: Angelo Miguel
authors.initials: AM
authors.lastname: Figueiredo
authors.forename: Geoffrey R
authors.initials: GR
authors.lastname: Moore
authors.forename: Sara B-M
authors.initials: SB
authors.lastname: Whittaker
mesh_terms: D003087:Colicins / Q000737:chemistry* / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy; D017510:Protein Folding; D017433:Protein Structure, Secondary; D013816:Thermodynamics
chemical_list: D003087:Colicins