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Structural Biology: A Century-long Journey into an Unseen World.

Curry S - Interdiscip Sci Rev (2015)

Bottom Line: Since then the toolbox of structural biology has been augmented by other physical techniques, including nuclear magnetic resonance spectroscopy, electron microscopy, and solution scattering of X-rays and neutrons.Together these have transformed our understanding of the molecular basis of life.Here I review the major and most recent developments in structural biology that have brought us to the threshold of a landscape of astonishing molecular complexity.

View Article: PubMed Central - PubMed

Affiliation: Department of Life Sciences, Imperial College London, UK.

ABSTRACT

When the first atomic structures of salt crystals were determined by the Braggs in 1912-1913, the analytical power of X-ray crystallography was immediately evident. Within a few decades the technique was being applied to the more complex molecules of chemistry and biology and is rightly regarded as the foundation stone of structural biology, a field that emerged in the 1950s when X-ray diffraction analysis revealed the atomic architecture of DNA and protein molecules. Since then the toolbox of structural biology has been augmented by other physical techniques, including nuclear magnetic resonance spectroscopy, electron microscopy, and solution scattering of X-rays and neutrons. Together these have transformed our understanding of the molecular basis of life. Here I review the major and most recent developments in structural biology that have brought us to the threshold of a landscape of astonishing molecular complexity.

No MeSH data available.


Related in: MedlinePlus

NMR: (a) a 1D spectrum showing the proton (1H) chemical shifts recorded for a protein molecule, (b) a 2D spectrum showing the correlation of NMR chemical shifts between bonded 1H and 15N nuclei in a protein structure, (c) a best-fit ensemble of protein structures calculated from NMR data; for clarity only the protein backbone is shown.
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Figure 0002: NMR: (a) a 1D spectrum showing the proton (1H) chemical shifts recorded for a protein molecule, (b) a 2D spectrum showing the correlation of NMR chemical shifts between bonded 1H and 15N nuclei in a protein structure, (c) a best-fit ensemble of protein structures calculated from NMR data; for clarity only the protein backbone is shown.

Mentions: Although the physical principles underlying NMR are relatively simple, putting them into practice is a complex business and no attempt will be made here to give detailed description (Kwan et al. 2011, Marion 2013). What is particularly striking about the method is the indirectness of the process of information extraction. A one-dimensional (1D) NMR spectrum of a protein, which typically simply captures the frequencies at which its H atoms resonate, gives a good idea of the dispersion of chemical shifts due to the distinct stereochemical environments of each nucleus (Figure 2a). For protein structure determinations chemical shift measurements are made in 2D experiments (Figure 2b), where the magnetization excited in one nucleus can be transferred to another of a different atomic species (e.g. H-N or H-C), or 3D experiments where the transfer is between three distinct species, most commonly H, C, and N.


Structural Biology: A Century-long Journey into an Unseen World.

Curry S - Interdiscip Sci Rev (2015)

NMR: (a) a 1D spectrum showing the proton (1H) chemical shifts recorded for a protein molecule, (b) a 2D spectrum showing the correlation of NMR chemical shifts between bonded 1H and 15N nuclei in a protein structure, (c) a best-fit ensemble of protein structures calculated from NMR data; for clarity only the protein backbone is shown.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4697198&req=5

Figure 0002: NMR: (a) a 1D spectrum showing the proton (1H) chemical shifts recorded for a protein molecule, (b) a 2D spectrum showing the correlation of NMR chemical shifts between bonded 1H and 15N nuclei in a protein structure, (c) a best-fit ensemble of protein structures calculated from NMR data; for clarity only the protein backbone is shown.
Mentions: Although the physical principles underlying NMR are relatively simple, putting them into practice is a complex business and no attempt will be made here to give detailed description (Kwan et al. 2011, Marion 2013). What is particularly striking about the method is the indirectness of the process of information extraction. A one-dimensional (1D) NMR spectrum of a protein, which typically simply captures the frequencies at which its H atoms resonate, gives a good idea of the dispersion of chemical shifts due to the distinct stereochemical environments of each nucleus (Figure 2a). For protein structure determinations chemical shift measurements are made in 2D experiments (Figure 2b), where the magnetization excited in one nucleus can be transferred to another of a different atomic species (e.g. H-N or H-C), or 3D experiments where the transfer is between three distinct species, most commonly H, C, and N.

Bottom Line: Since then the toolbox of structural biology has been augmented by other physical techniques, including nuclear magnetic resonance spectroscopy, electron microscopy, and solution scattering of X-rays and neutrons.Together these have transformed our understanding of the molecular basis of life.Here I review the major and most recent developments in structural biology that have brought us to the threshold of a landscape of astonishing molecular complexity.

View Article: PubMed Central - PubMed

Affiliation: Department of Life Sciences, Imperial College London, UK.

ABSTRACT

When the first atomic structures of salt crystals were determined by the Braggs in 1912-1913, the analytical power of X-ray crystallography was immediately evident. Within a few decades the technique was being applied to the more complex molecules of chemistry and biology and is rightly regarded as the foundation stone of structural biology, a field that emerged in the 1950s when X-ray diffraction analysis revealed the atomic architecture of DNA and protein molecules. Since then the toolbox of structural biology has been augmented by other physical techniques, including nuclear magnetic resonance spectroscopy, electron microscopy, and solution scattering of X-rays and neutrons. Together these have transformed our understanding of the molecular basis of life. Here I review the major and most recent developments in structural biology that have brought us to the threshold of a landscape of astonishing molecular complexity.

No MeSH data available.


Related in: MedlinePlus