NDLI: Importance of α–helix N–capping motif in stabilization of ββα fold

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Importance of α–helix N–capping motif in stabilization of ββα fold

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Importance of α–helix N–capping motif in stabilization of ββα fold

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Cierpicki, Tomasz Otlewski, Jacek Koscielska-Kasprzak, Katarzyna
Description	Country affiliation: Poland Author Affiliation: Koscielska-Kasprzak K ( Laboratory of Protein Engineering, Institute of Biochemistry and Molecular Biology, University of Wroclaw, Tamka 2, 50-137 Wroclaw, Poland.)
Abstract	FSD-1 (full sequence design 1) is a protein folded in a betabetaalpha motif, designed on the basis of the second zinc finger domain of Zif268 by a substitution of its metal coordination site with a hydrophobic core. In this work, we analyzed the possibility of introducing the DNA recognition motif of the template zinc finger (S(13)RSDH(17)) into FSD-1 sequence in order to obtain a small DNA-binding module devoid of cross-link(s) or metal cofactors. The hybrid protein was unfolded, as judged by CD and NMR criteria. To reveal the role of each of the five amino acids, which form the N-capping motif of the alpha-helix, we analyzed conformational and stability properties of eight FSD-1 mutants. We used a shielded methyl group of Leu 18 and a CD signal at 215 nm as a convenient measure of the folded state. Glu 17-->His substitution at the N(3) in S(13)NEKE(17) variant decreased the folded structure content from 90% to 25% (equivalent to 1.8 kcal * mole(-1) destabilization) by disruption of N-capping interactions, and had the most significant effect among single mutants studied here. The N(cap) Asn 14 substitution with Arg considerably decreased stability, reducing structure content from 90% to 40% (1.4 kcal * mole(-1) destabilization) by disruption of a helix-capping hydrogen bond and destabilization of a helix macrodipole. The N(1) Glu 15-->Ser mutation also produced a considerable effect (1.0 kcal * mole(-1) destabilization), again emphasizing the significance of electrostatic interactions in alpha-helix stabilization.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	6
Volume Number	12
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2003-06-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Dna-binding Proteins Chemistry Protein Folding Protein Structure, Secondary Transcription Factors Amides Amino Acid Motifs Amino Acid Sequence Amino Acid Substitution Circular Dichroism Hydrogen-ion Concentration Models, Molecular Mutation Nuclear Magnetic Resonance, Biomolecular Peptides Genetics Thermodynamics Zinc Fingers Research Support, Non-u.s. Gov't Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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