Challenges in NMR-based structural genomics

Shih Che Sue, Chi Fon Chang, Yao Te Huang, Ching Yu Chou, Tai Huang Huang

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Understanding the functions of the vast number of proteins encoded in many genomes that have been completely sequenced recently is the main challenge for biologists in the post-genomics era. Since the function of a protein is determined by its exact three-dimensional structure it is paramount to determine the 3D structures of all proteins. This need has driven structural biologists to undertake the structural genomics project aimed at determining the structures of all known proteins. Several centers for structural genomics studies have been established throughout the world. Nuclear magnetic resonance (NMR) spectroscopy has played a major role in determining protein structures in atomic details and in a physiologically relevant solution state. Since the number of new genes being discovered daily far exceeds the number of structures determined by both NMR and X-ray crystallography, a high-throughput method for speeding up the process of protein structure determination is essential for the success of the structural genomics effort. In this article we will describe NMR methods currently being employed for protein structure determination. We will also describe methods under development which may drastically increase the throughput, as well as point out areas where opportunities exist for biophysicists to make significant contribution in this important field.

Original languageEnglish
Pages (from-to)12-27
Number of pages16
JournalPhysica A: Statistical Mechanics and its Applications
Volume350
Issue number1
DOIs
Publication statusPublished - 2005 May 1

Fingerprint

Nuclear Magnetic Resonance
Genomics
Protein Structure
proteins
Protein
nuclear magnetic resonance
High Throughput
Spectroscopy
Exceed
Genome
Throughput
Gene
genome
magnetic resonance spectroscopy
Three-dimensional
genes
crystallography

Keywords

  • NMR
  • Protein
  • Structural genomics
  • Structure

ASJC Scopus subject areas

  • Statistics and Probability
  • Condensed Matter Physics

Cite this

Challenges in NMR-based structural genomics. / Sue, Shih Che; Chang, Chi Fon; Huang, Yao Te; Chou, Ching Yu; Huang, Tai Huang.

In: Physica A: Statistical Mechanics and its Applications, Vol. 350, No. 1, 01.05.2005, p. 12-27.

Research output: Contribution to journalArticle

Sue, Shih Che ; Chang, Chi Fon ; Huang, Yao Te ; Chou, Ching Yu ; Huang, Tai Huang. / Challenges in NMR-based structural genomics. In: Physica A: Statistical Mechanics and its Applications. 2005 ; Vol. 350, No. 1. pp. 12-27.
@article{91e39d371b764ade9b08fc41f12a6da3,
title = "Challenges in NMR-based structural genomics",
abstract = "Understanding the functions of the vast number of proteins encoded in many genomes that have been completely sequenced recently is the main challenge for biologists in the post-genomics era. Since the function of a protein is determined by its exact three-dimensional structure it is paramount to determine the 3D structures of all proteins. This need has driven structural biologists to undertake the structural genomics project aimed at determining the structures of all known proteins. Several centers for structural genomics studies have been established throughout the world. Nuclear magnetic resonance (NMR) spectroscopy has played a major role in determining protein structures in atomic details and in a physiologically relevant solution state. Since the number of new genes being discovered daily far exceeds the number of structures determined by both NMR and X-ray crystallography, a high-throughput method for speeding up the process of protein structure determination is essential for the success of the structural genomics effort. In this article we will describe NMR methods currently being employed for protein structure determination. We will also describe methods under development which may drastically increase the throughput, as well as point out areas where opportunities exist for biophysicists to make significant contribution in this important field.",
keywords = "NMR, Protein, Structural genomics, Structure",
author = "Sue, {Shih Che} and Chang, {Chi Fon} and Huang, {Yao Te} and Chou, {Ching Yu} and Huang, {Tai Huang}",
year = "2005",
month = "5",
day = "1",
doi = "10.1016/j.physa.2004.11.022",
language = "English",
volume = "350",
pages = "12--27",
journal = "Physica A: Statistical Mechanics and its Applications",
issn = "0378-4371",
publisher = "Elsevier",
number = "1",

}

TY - JOUR

T1 - Challenges in NMR-based structural genomics

AU - Sue, Shih Che

AU - Chang, Chi Fon

AU - Huang, Yao Te

AU - Chou, Ching Yu

AU - Huang, Tai Huang

PY - 2005/5/1

Y1 - 2005/5/1

N2 - Understanding the functions of the vast number of proteins encoded in many genomes that have been completely sequenced recently is the main challenge for biologists in the post-genomics era. Since the function of a protein is determined by its exact three-dimensional structure it is paramount to determine the 3D structures of all proteins. This need has driven structural biologists to undertake the structural genomics project aimed at determining the structures of all known proteins. Several centers for structural genomics studies have been established throughout the world. Nuclear magnetic resonance (NMR) spectroscopy has played a major role in determining protein structures in atomic details and in a physiologically relevant solution state. Since the number of new genes being discovered daily far exceeds the number of structures determined by both NMR and X-ray crystallography, a high-throughput method for speeding up the process of protein structure determination is essential for the success of the structural genomics effort. In this article we will describe NMR methods currently being employed for protein structure determination. We will also describe methods under development which may drastically increase the throughput, as well as point out areas where opportunities exist for biophysicists to make significant contribution in this important field.

AB - Understanding the functions of the vast number of proteins encoded in many genomes that have been completely sequenced recently is the main challenge for biologists in the post-genomics era. Since the function of a protein is determined by its exact three-dimensional structure it is paramount to determine the 3D structures of all proteins. This need has driven structural biologists to undertake the structural genomics project aimed at determining the structures of all known proteins. Several centers for structural genomics studies have been established throughout the world. Nuclear magnetic resonance (NMR) spectroscopy has played a major role in determining protein structures in atomic details and in a physiologically relevant solution state. Since the number of new genes being discovered daily far exceeds the number of structures determined by both NMR and X-ray crystallography, a high-throughput method for speeding up the process of protein structure determination is essential for the success of the structural genomics effort. In this article we will describe NMR methods currently being employed for protein structure determination. We will also describe methods under development which may drastically increase the throughput, as well as point out areas where opportunities exist for biophysicists to make significant contribution in this important field.

KW - NMR

KW - Protein

KW - Structural genomics

KW - Structure

UR - http://www.scopus.com/inward/record.url?scp=14644422688&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=14644422688&partnerID=8YFLogxK

U2 - 10.1016/j.physa.2004.11.022

DO - 10.1016/j.physa.2004.11.022

M3 - Article

AN - SCOPUS:14644422688

VL - 350

SP - 12

EP - 27

JO - Physica A: Statistical Mechanics and its Applications

JF - Physica A: Statistical Mechanics and its Applications

SN - 0378-4371

IS - 1

ER -