NDLI: Effect of the N3 residue on the stability of the alpha-helix.

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Effect of the N3 residue on the stability of the alpha-helix.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Iqbalsyah, Teuku M. Doig, Andrew J.
Description	Country affiliation: United kingdom Author Affiliation: Iqbalsyah TM ( Department of Biomolecular Sciences, University of Manchester Institute of Science and Technology (UMIST), Manchester M60 1QD, UK.)
Abstract	N3 is the third position from the N terminus in the alpha-helix with helical backbone dihedral angles. All 20 amino acids have been placed in the N3 position of a synthetic helical peptide (CH(3)CO-[AAX AAAAKAAAAKAGY]-NH(2)) and the helix content measured by circular dichroism spectroscopy at 273 K. The dependence of peptide helicity on N3 residue identity has been used to determine a free energy scale by analysis with a modified Lifson-Roig helix coil theory that includes a parameter for the N3 energy (n3). The most stabilizing residues at N3 in rank order are Ala, Glu, Met/Ile, Leu, Lys, Ser, Gln, Thr, Tyr, Phe, Asp, His, and Trp. Free energies for the most destabilizing residues (Cys, Gly, Asn, Arg, and Pro) could not be fitted. The results correlate with N1, N2, and helix interior energies and not at all with N-cap preferences. This completes our work on studying the structural and energetic preferences of the amino acids for the N-terminal positions of the alpha-helix. These results can be used to rationally modify protein stability, help design helices, and improve prediction of helix location and stability.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	1
Volume Number	13
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2004-01-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Amino Acids Chemistry Peptides Chemical Synthesis Protein Structure, Secondary Algorithms Amino Acid Sequence Chromatography, High Pressure Liquid Circular Dichroism Enzyme Stability Hot Temperature Hydrogen-ion Concentration Isolation & Purification Protein Folding Thermodynamics Titrimetry Comparative Study Research Support, Non-u.s. Gov't Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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