NDLI: The role of context on alpha-helix stabilization: host-guest analysis in a mixed background peptide model.

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The role of context on alpha-helix stabilization: host-guest analysis in a mixed background peptide model.

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The role of context on alpha-helix stabilization: host-guest analysis in a mixed background peptide model.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Spek, E. J. Yang, J. Kallenbach, N. R. Gong, Y. Zhou, H.
Description	Country affiliation: United States Author Affiliation: Yang J ( Department of Chemistry, New York University, New York 10003, USA.)
Abstract	The helix content of a series of peptides containing single substitutions of the 20 natural amino acids in a new designed host sequence, succinyl-YSEEEEKAKKAXAEEAEKKKK-NH2, has been determined using CD spectroscopy. This host is related to one previously studied, in which triple amino acid substitutions were introduced into a background of Glu-Lys blocks completely lacking alanine. The resulting free energies show that only Ala and Glu- prove to be helix stabilizing, while all other side chains are neutral or destabilizing. This agrees with results from studies of alanine-rich peptide modela, but not the previous Glu-Lys block oligomers in which Leu and Met also stabilize helix. The helix propensity scale derived from the previous block oligomers correlated well with the frequencies of occurrence of different side chains in helical sequences of proteins, whereas the values from the present series do not. The role of context in determining scales of helix propensity values is discussed, and the ability of algorithms designed to predict helix structure from sequence is compared.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	6
Volume Number	6
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1997-06-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Peptides Chemistry Protein Structure, Secondary Algorithms Amino Acid Sequence Circular Dichroism Magnetic Resonance Spectroscopy Molecular Sequence Data Drug Effects Sodium Chloride Pharmacology Temperature Thermodynamics Comparative Study Research Support, Non-u.s. Gov't Research Support, U.s. Gov't, P.h.s. Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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