Engineering Protein Orientation at Surfaces to Control Macromolecular Recognition Events

Mark A. McLean; Patrick S. Stayton; Stephen G. Sligar

doi:10.1021/ac00067a021

Engineering Protein Orientation at Surfaces to Control Macromolecular Recognition Events

Mark A. McLean, Patrick S. Stayton, Stephen G. Sligar

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

Abstract

In this report we demonstrate that heterologous protein-protein interactions can be controlled at an immobilization surface by genetically engineering an appropriately de novo designed attachment point on the protein surface.

Original language	English (US)
Pages (from-to)	2676-2678
Number of pages	3
Journal	Analytical Chemistry
Volume	65
Issue number	19
DOIs	https://doi.org/10.1021/ac00067a021
State	Published - Oct 1 1993

ASJC Scopus subject areas

Analytical Chemistry

Online availability

10.1021/ac00067a021

Library availability

Discover UIUC Full Text

Cite this

@article{8957ecb00e254dff9aa4d5aca004c46b,

title = "Engineering Protein Orientation at Surfaces to Control Macromolecular Recognition Events",

abstract = "In this report we demonstrate that heterologous protein-protein interactions can be controlled at an immobilization surface by genetically engineering an appropriately de novo designed attachment point on the protein surface.",

author = "McLean, {Mark A.} and Stayton, {Patrick S.} and Sligar, {Stephen G.}",

year = "1993",

month = oct,

day = "1",

doi = "10.1021/ac00067a021",

language = "English (US)",

volume = "65",

pages = "2676--2678",

journal = "Analytical Chemistry",

issn = "0003-2700",

number = "19",

}

TY - JOUR

T1 - Engineering Protein Orientation at Surfaces to Control Macromolecular Recognition Events

AU - McLean, Mark A.

AU - Stayton, Patrick S.

AU - Sligar, Stephen G.

PY - 1993/10/1

Y1 - 1993/10/1

N2 - In this report we demonstrate that heterologous protein-protein interactions can be controlled at an immobilization surface by genetically engineering an appropriately de novo designed attachment point on the protein surface.

AB - In this report we demonstrate that heterologous protein-protein interactions can be controlled at an immobilization surface by genetically engineering an appropriately de novo designed attachment point on the protein surface.

UR - http://www.scopus.com/inward/record.url?scp=0027679323&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027679323&partnerID=8YFLogxK

U2 - 10.1021/ac00067a021

DO - 10.1021/ac00067a021

M3 - Article

C2 - 8238945

AN - SCOPUS:0027679323

SN - 0003-2700

VL - 65

SP - 2676

EP - 2678

JO - Analytical Chemistry

JF - Analytical Chemistry

IS - 19

ER -

Engineering Protein Orientation at Surfaces to Control Macromolecular Recognition Events

Abstract

ASJC Scopus subject areas

Online availability

Library availability

Related links

Fingerprint

Cite this