Membrane proteins by accident or design

John Simms; Paula J Booth

doi:10.1016/j.cbpa.2013.10.005

Membrane proteins by accident or design

John Simms, Paula J Booth

School of Nursing, Midwifery and Health

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

5 Citations (Scopus)

Abstract

Protein design is a valuable tool to create bespoke proteins with desired properties as well as for investigating sequence, structure and function relationships. Membrane protein design is a burgeoning field that is hampered by the lack of high-resolution structural information. In spite of these shortcomings, computational methods have offered a route towards blueprints for these hydrophobic proteins. Advances in structural scoring and sampling methods are enabling more accurate predictions of a folded structure from the primary amino acid sequence. This review highlights a number of novel studies focusing on the methods and information used to successfully design membrane proteins.

Original language	English
Pages (from-to)	976-981
Number of pages	6
Journal	Current Opinion in Chemical Biology
Volume	17
Issue number	6
DOIs	https://doi.org/10.1016/j.cbpa.2013.10.005
Publication status	Published - Dec 2013

Keywords

Amino Acid Sequence
Animals
Computer Simulation
Humans
Membrane Proteins
Models, Molecular
Molecular Sequence Data
Protein Conformation
Protein Engineering
Protein Folding
Journal Article
Research Support, Non-U.S. Gov't
Review

Access to Document

10.1016/j.cbpa.2013.10.005

Cite this

@article{64a0227feabd4642a5adf7e7a6de188c,

title = "Membrane proteins by accident or design",

abstract = "Protein design is a valuable tool to create bespoke proteins with desired properties as well as for investigating sequence, structure and function relationships. Membrane protein design is a burgeoning field that is hampered by the lack of high-resolution structural information. In spite of these shortcomings, computational methods have offered a route towards blueprints for these hydrophobic proteins. Advances in structural scoring and sampling methods are enabling more accurate predictions of a folded structure from the primary amino acid sequence. This review highlights a number of novel studies focusing on the methods and information used to successfully design membrane proteins.",

keywords = "Amino Acid Sequence, Animals, Computer Simulation, Humans, Membrane Proteins, Models, Molecular, Molecular Sequence Data, Protein Conformation, Protein Engineering, Protein Folding, Journal Article, Research Support, Non-U.S. Gov't, Review",

author = "John Simms and Booth, {Paula J}",

year = "2013",

month = dec,

doi = "10.1016/j.cbpa.2013.10.005",

language = "English",

volume = "17",

pages = "976--981",

journal = "Current Opinion in Chemical Biology",

issn = "1367-5931",

publisher = "Elsevier",

number = "6",

}

TY - JOUR

T1 - Membrane proteins by accident or design

AU - Simms, John

AU - Booth, Paula J

PY - 2013/12

Y1 - 2013/12

N2 - Protein design is a valuable tool to create bespoke proteins with desired properties as well as for investigating sequence, structure and function relationships. Membrane protein design is a burgeoning field that is hampered by the lack of high-resolution structural information. In spite of these shortcomings, computational methods have offered a route towards blueprints for these hydrophobic proteins. Advances in structural scoring and sampling methods are enabling more accurate predictions of a folded structure from the primary amino acid sequence. This review highlights a number of novel studies focusing on the methods and information used to successfully design membrane proteins.

AB - Protein design is a valuable tool to create bespoke proteins with desired properties as well as for investigating sequence, structure and function relationships. Membrane protein design is a burgeoning field that is hampered by the lack of high-resolution structural information. In spite of these shortcomings, computational methods have offered a route towards blueprints for these hydrophobic proteins. Advances in structural scoring and sampling methods are enabling more accurate predictions of a folded structure from the primary amino acid sequence. This review highlights a number of novel studies focusing on the methods and information used to successfully design membrane proteins.

KW - Amino Acid Sequence

KW - Animals

KW - Computer Simulation

KW - Humans

KW - Membrane Proteins

KW - Models, Molecular

KW - Molecular Sequence Data

KW - Protein Conformation

KW - Protein Engineering

KW - Protein Folding

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

KW - Review

U2 - 10.1016/j.cbpa.2013.10.005

DO - 10.1016/j.cbpa.2013.10.005

M3 - Review article

C2 - 24466578

SN - 1367-5931

VL - 17

SP - 976

EP - 981

JO - Current Opinion in Chemical Biology

JF - Current Opinion in Chemical Biology

IS - 6

ER -

Membrane proteins by accident or design

Abstract

Keywords

Access to Document

Fingerprint

Cite this