Protein recognition motifs: design of peptidomimetics of helix surfaces.

Protein recognition motifs: design of peptidomimetics of helix surfaces. Research Abstract Details 

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Protein recognition motifs: design of peptidomimetics of helix surfaces. Abstract Text:

Ye Che,Bernard R Brooks,Garland R Marshall,

Helices represent one of the most common recognition motifs in proteins. The design of nonpeptidic scaffolds, such as the 3,2',2''-tris-substituted terphenyl, that can imitate the side-chain orientation along one face of an alpha-helix potentially provides an effective means to modulate helix-recognition functions. Here, based on theoretical arguments, we described novel alpha-helix mimetics which are more effective than the terphenyl at constraining the aryl-aryl torsion angles to those associated with structures suitable for mimicking the alpha-helical twist for side-chain orientation and for superimposing the side chains of residues i, i + 3 or i + 4, i + 7 when compared with the alpha-beta side-chain vectors of the regular alpha-helix with an improved root mean square deviation (RMSD) of approximately 0.5 A. In addition, this study suggests that rotamer distributions around the C(alpha)--C(beta) bonds of these helix mimetics are similar to those of alpha-helices, except that these rotamer distributions show an approximately 60 degrees shift compared to those of alpha-helices when the mimetic axis is superimposed upon the helix axis. This change in rotamer orientation complicates mimicry of the helix surface.

Protein recognition motifs: design of peptidomimetics of helix surfaces. Publishing Authors By Initials

Y Che,BR Brooks,GR Marshall,

For similar organic chemicals: hydrocarbons: hydrocarbons, cyclic: hydrocarbons, aromatic: benzene derivatives: terphenyl compounds research abstracts see: organic chemicals: hydrocarbons: hydrocarbons, cyclic: hydrocarbons, aromatic: benzene derivatives: terphenyl compounds research

PUBMED ID PMID:

MEDLINE DATE:

Protein recognition motifs: design of peptidomimetics of helix surfaces. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Intr

Journal: Biopolymers

VOLUME: 86

Page Numbers: 288-97

Journal Abbreviation: Biopolymers

ISSN: 0006-3525

DAY: 3

MONTH: Jul

YEAR: 2007

Protein recognition motifs: design of peptidomimetics of helix surfaces. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 372525

Protein recognition motifs: design of peptidomimetics of helix surfaces. Keywords Mesh Terms:

KEYWORDS: Terphenyl Compounds

MESH TERMS: chemistry

Chemical & Substance for Abstract: Protein recognition motifs: design of peptidomimetics of helix surfaces. Information

Substance Name: Terphenyl Compounds

Registry Number: 0

Grant and Affiliation Information for Protein recognition motifs: design of peptidomimetics of helix surfaces.

AFFILIATION: Laboratory of Computational Biology, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA. chey@nhlbi.nih.gov

Country: United States

AGENCY: United States NIGMS

GRANT: GM 68460

ACRONYM: GM

MEDLINETA: Biopolymers

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