Design and characterization of a homodimeric antiparallel coiled coil

Daniel G. Gurnon; Jennifer A. Whitaker; Martha G. Oakley

doi:10.1021/ja0357590

Design and characterization of a homodimeric antiparallel coiled coil

Daniel G. Gurnon, Jennifer A. Whitaker, Martha G. Oakley

General Internal Medicine

Research output: Contribution to journal › Article › peer-review

55 Scopus citations

Abstract

We report the first successful design of a self-associating antiparallel coiled coil, APH. The simultaneous application of Coulombic and hydrophobic components results in a decided preference for the antiparallel alignment as judged by HPLC, sedimentation equilibrium, and chemical denaturation data. The designed peptide is of comparable stability to naturally occurring leucine zipper peptides and can be expressed in bacteria. These properties of APH suggest potential in vivo protein fusion and biomaterials applications.

Original language	English (US)
Pages (from-to)	7518-7519
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	125
Issue number	25
DOIs	https://doi.org/10.1021/ja0357590
State	Published - Jun 25 2003

ASJC Scopus subject areas

Catalysis
Chemistry(all)
Biochemistry
Colloid and Surface Chemistry

Access to Document

10.1021/ja0357590

Cite this

@article{35b1438d92cb444aa65894d88f0219b5,

title = "Design and characterization of a homodimeric antiparallel coiled coil",

abstract = "We report the first successful design of a self-associating antiparallel coiled coil, APH. The simultaneous application of Coulombic and hydrophobic components results in a decided preference for the antiparallel alignment as judged by HPLC, sedimentation equilibrium, and chemical denaturation data. The designed peptide is of comparable stability to naturally occurring leucine zipper peptides and can be expressed in bacteria. These properties of APH suggest potential in vivo protein fusion and biomaterials applications.",

author = "Gurnon, {Daniel G.} and Whitaker, {Jennifer A.} and Oakley, {Martha G.}",

year = "2003",

month = jun,

day = "25",

doi = "10.1021/ja0357590",

language = "English (US)",

volume = "125",

pages = "7518--7519",

journal = "Journal of the American Chemical Society",

issn = "0002-7863",

publisher = "American Chemical Society",

number = "25",

}

TY - JOUR

T1 - Design and characterization of a homodimeric antiparallel coiled coil

AU - Gurnon, Daniel G.

AU - Whitaker, Jennifer A.

AU - Oakley, Martha G.

PY - 2003/6/25

Y1 - 2003/6/25

N2 - We report the first successful design of a self-associating antiparallel coiled coil, APH. The simultaneous application of Coulombic and hydrophobic components results in a decided preference for the antiparallel alignment as judged by HPLC, sedimentation equilibrium, and chemical denaturation data. The designed peptide is of comparable stability to naturally occurring leucine zipper peptides and can be expressed in bacteria. These properties of APH suggest potential in vivo protein fusion and biomaterials applications.

AB - We report the first successful design of a self-associating antiparallel coiled coil, APH. The simultaneous application of Coulombic and hydrophobic components results in a decided preference for the antiparallel alignment as judged by HPLC, sedimentation equilibrium, and chemical denaturation data. The designed peptide is of comparable stability to naturally occurring leucine zipper peptides and can be expressed in bacteria. These properties of APH suggest potential in vivo protein fusion and biomaterials applications.

UR - http://www.scopus.com/inward/record.url?scp=0038546882&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0038546882&partnerID=8YFLogxK

U2 - 10.1021/ja0357590

DO - 10.1021/ja0357590

M3 - Article

C2 - 12812483

AN - SCOPUS:0038546882

SN - 0002-7863

VL - 125

SP - 7518

EP - 7519

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

IS - 25

ER -

Design and characterization of a homodimeric antiparallel coiled coil

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this