Semisynthetic proteins in mechanistic studies: using chemistry to go where nature can't

Jean Philippe Pellois; Tom W. Muir

doi:10.1016/j.cbpa.2006.08.016

Semisynthetic proteins in mechanistic studies: using chemistry to go where nature can't

Jean Philippe Pellois
, Tom W. Muir

Research output: Contribution to journal › Review article › peer-review

47 Scopus citations

Abstract

The manipulation of the chemical structure of proteins beyond what is feasible with standard genetics, offers a powerful strategy to investigate protein mechanisms. By allowing the incorporation of biophysical probes, unnatural amino acids, and post-translational modifications in proteins, chemistry-driven approaches have greatly contributed to the understanding of the molecular basis of protein function.

Original language	English (US)
Pages (from-to)	487-491
Number of pages	5
Journal	Current Opinion in Chemical Biology
Volume	10
Issue number	5
DOIs	https://doi.org/10.1016/j.cbpa.2006.08.016
State	Published - Oct 2006
Externally published	Yes

All Science Journal Classification (ASJC) codes

Analytical Chemistry
Biochemistry

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10.1016/j.cbpa.2006.08.016

Cite this

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title = "Semisynthetic proteins in mechanistic studies: using chemistry to go where nature can't",

abstract = "The manipulation of the chemical structure of proteins beyond what is feasible with standard genetics, offers a powerful strategy to investigate protein mechanisms. By allowing the incorporation of biophysical probes, unnatural amino acids, and post-translational modifications in proteins, chemistry-driven approaches have greatly contributed to the understanding of the molecular basis of protein function.",

author = "Pellois, \{Jean Philippe\} and Muir, \{Tom W.\}",

note = "Funding Information: The authors acknowledge the support of the National Institutes of Health.",

year = "2006",

month = oct,

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T2 - using chemistry to go where nature can't

AU - Pellois, Jean Philippe

AU - Muir, Tom W.

N1 - Funding Information: The authors acknowledge the support of the National Institutes of Health.

PY - 2006/10

Y1 - 2006/10

N2 - The manipulation of the chemical structure of proteins beyond what is feasible with standard genetics, offers a powerful strategy to investigate protein mechanisms. By allowing the incorporation of biophysical probes, unnatural amino acids, and post-translational modifications in proteins, chemistry-driven approaches have greatly contributed to the understanding of the molecular basis of protein function.

AB - The manipulation of the chemical structure of proteins beyond what is feasible with standard genetics, offers a powerful strategy to investigate protein mechanisms. By allowing the incorporation of biophysical probes, unnatural amino acids, and post-translational modifications in proteins, chemistry-driven approaches have greatly contributed to the understanding of the molecular basis of protein function.

UR - https://www.scopus.com/pages/publications/33748552028

UR - https://www.scopus.com/pages/publications/33748552028#tab=citedBy

U2 - 10.1016/j.cbpa.2006.08.016

DO - 10.1016/j.cbpa.2006.08.016

M3 - Review article

C2 - 16935551

AN - SCOPUS:33748552028

SN - 1367-5931

VL - 10

SP - 487

EP - 491

JO - Current Opinion in Chemical Biology

JF - Current Opinion in Chemical Biology

IS - 5

ER -

Semisynthetic proteins in mechanistic studies: using chemistry to go where nature can't

Abstract

All Science Journal Classification (ASJC) codes

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