Towards an understanding of structure-function relationships of elongation factor Tu.

O Wiborg; C Andersen; Charlotte Rohde Knudsen; T J Kristensen; Brian F. C. Clark

Towards an understanding of structure-function relationships of elongation factor Tu.

O Wiborg, C Andersen, Charlotte Rohde Knudsen, T J Kristensen, Brian F. C. Clark

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

11 Citations (Scopus)

Abstract

In light of the recently determined structure of elongation factor Tu, and taking into account chemical studies mapping functional sites, a number of residues have been selected for site-directed mutagenesis studies. Gly94, Gly126, His66, His118, Lys89 and Asp90 have each been point-mutated. Preliminary in vitro characterization data are presented.
Udgivelsesdato: 1994-Feb

Original language	English
Journal	Biotechnology and Applied Biochemistry
Volume	19 ( Pt 1)
Pages (from-to)	3-15
Number of pages	12
ISSN	0885-4513
Publication status	Published - 1994

Keywords

Amino Acids
Escherichia coli
Models, Molecular
Mutagenesis, Site-Directed
Peptide Elongation Factor Tu
Point Mutation
Protein Conformation
Protein Structure, Secondary
Structure-Activity Relationship

Cite this

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title = "Towards an understanding of structure-function relationships of elongation factor Tu.",

abstract = "In light of the recently determined structure of elongation factor Tu, and taking into account chemical studies mapping functional sites, a number of residues have been selected for site-directed mutagenesis studies. Gly94, Gly126, His66, His118, Lys89 and Asp90 have each been point-mutated. Preliminary in vitro characterization data are presented. Udgivelsesdato: 1994-Feb",

keywords = "Amino Acids, Escherichia coli, Models, Molecular, Mutagenesis, Site-Directed, Peptide Elongation Factor Tu, Point Mutation, Protein Conformation, Protein Structure, Secondary, Structure-Activity Relationship",

author = "O Wiborg and C Andersen and Knudsen, {Charlotte Rohde} and Kristensen, {T J} and Clark, {Brian F. C.}",

year = "1994",

language = "English",

volume = "19 ( Pt 1)",

pages = "3--15",

journal = "Biotechnology and Applied Biochemistry",

issn = "0885-4513",

publisher = "Wiley-Blackwell",

}

TY - JOUR

T1 - Towards an understanding of structure-function relationships of elongation factor Tu.

AU - Wiborg, O

AU - Andersen, C

AU - Knudsen, Charlotte Rohde

AU - Kristensen, T J

AU - Clark, Brian F. C.

PY - 1994

Y1 - 1994

N2 - In light of the recently determined structure of elongation factor Tu, and taking into account chemical studies mapping functional sites, a number of residues have been selected for site-directed mutagenesis studies. Gly94, Gly126, His66, His118, Lys89 and Asp90 have each been point-mutated. Preliminary in vitro characterization data are presented. Udgivelsesdato: 1994-Feb

AB - In light of the recently determined structure of elongation factor Tu, and taking into account chemical studies mapping functional sites, a number of residues have been selected for site-directed mutagenesis studies. Gly94, Gly126, His66, His118, Lys89 and Asp90 have each been point-mutated. Preliminary in vitro characterization data are presented. Udgivelsesdato: 1994-Feb

KW - Amino Acids

KW - Escherichia coli

KW - Models, Molecular

KW - Mutagenesis, Site-Directed

KW - Peptide Elongation Factor Tu

KW - Point Mutation

KW - Protein Conformation

KW - Protein Structure, Secondary

KW - Structure-Activity Relationship

M3 - Journal article

C2 - 8136078

SN - 0885-4513

VL - 19 ( Pt 1)

SP - 3

EP - 15

JO - Biotechnology and Applied Biochemistry

JF - Biotechnology and Applied Biochemistry

ER -