- "Structural biology is a field that is many centuries old which, as defined by the Journal of Structural Biology, deals with structural analysis of living material (formed, composed of, and/or maintained and refined by living cells) at every level of organization."
The study of the three-dimensional structures of biological molecules and their interactions.
Biomolecules: Study of the 3D structures and functions of biological macromolecules, including proteins, nucleic acids, carbohydrates, and lipids. This can include topics such as amino acids, peptide bonds, and secondary and tertiary structures.
Crystallography: The use of X-ray crystallography to determine the 3D structures of biomolecules. This can involve learning about diffraction patterns, Bragg's Law, and the electron density map.
NMR spectroscopy: The use of nuclear magnetic resonance spectroscopy to study the structures and interactions of biomolecules in solution. This can include learning about chemical shifts, relaxation times, and NOE measurements.
Computational methods: The use of computational methods to model and study the structure and dynamics of biomolecules. This can include topics such as molecular dynamics simulations, homology modeling, and docking.
Enzyme kinetics: The study of the rates and mechanisms of enzymatic reactions. This can involve learning about factors that affect enzyme activity, such as temperature, pH, and substrate concentration.
Biophysical techniques: Other biophysical techniques that are commonly used in structural biology, including mass spectrometry, circular dichroism, and fluorescence spectroscopy.
Membrane proteins: Study of the structure and function of membrane proteins, which are involved in a range of cellular processes including signaling and transport.
Protein-ligand interactions: Study of the interactions between proteins and small molecules, including drugs and other ligands. This can involve learning about binding kinetics, affinity measurements, and structural studies of protein-ligand complexes.
Cell biology: Understanding of the role of structural biology techniques in answering questions related to cell biology, such as the structure and function of organelles and cytoskeletal elements.
Protein folding and misfolding: Study of the process of protein folding, as well as the causes and consequences of protein misfolding, which can lead to diseases such as Alzheimer's and Parkinson's.
X-ray scattering: The use of X-ray scattering techniques to study the structures of large biomolecular complexes, such as viruses and ribosomes.
Cryo-electron microscopy: The use of cryo-electron microscopy to study the structures of macromolecular complexes, including DNA, RNA, and proteins.
Drug discovery: Understanding of the role of structural biology techniques in the discovery and development of new drugs, including structure-based drug design.
Molecular evolution: Understanding of the role of structural biology in studying the evolution of biomolecules, including the identification of homologous structures and the use of phylogenetic methods.
X-ray crystallography: This involves analyzing the diffraction patterns created by X-rays on crystallized biological molecules to deduce their structure.
NMR spectroscopy: NMR (nuclear magnetic resonance) spectroscopy measures the magnetic properties of atoms to study the structure and dynamics of molecules in solution.
Cryo-electron microscopy: This involves analyzing frozen biological samples with an electron microscope, obtaining 3D images of the molecules and enabling their structure to be deduced.
Small-angle X-ray scattering (SAXS): SAXS measures the scattering of X-rays as they pass through a sample, allowing the dimensions and shape of the molecules to be estimated.
Molecular simulations: These use computational models to simulate the behavior of biological molecules, allowing researchers to study their interactions, dynamics, and structure.
Neutron scattering: This technique involves analyzing how neutron beams interact with biological molecules to obtain structural information.
Fluorescence resonance energy transfer (FRET): FRET measures the interaction between fluorescent molecules to obtain information about the structure and dynamics of biological molecules.
Circular dichroism (CD): CD measures the differential absorption of left- and right-handed circularly polarized light by chiral molecules, providing information on their structure and folding.
- "Early structural biologists throughout the 19th and early 20th centuries were primarily only able to study structures to the limit of the naked eye's visual acuity and through magnifying glasses and light microscopes."
- "The most prominent techniques are X-ray crystallography, nuclear magnetic resonance, and electron microscopy."
- "Through the discovery of X-rays and its applications to protein crystals, structural biology was revolutionized, as now scientists could obtain the three-dimensional structures of biological molecules in atomic detail."
- "Likewise, NMR spectroscopy allowed information about protein structure and dynamics to be obtained."
- "In the 21st century, electron microscopy also saw a drastic revolution with the development of more coherent electron sources, aberration correction for electron microscopes, and reconstruction software that enabled the successful implementation of high-resolution cryo-electron microscopy."
- "The field of structural biology expanded and also became a branch of molecular biology, biochemistry, and biophysics."
- "Molecular structure of biological macromolecules (especially proteins, made up of amino acids, RNA or DNA, made up of nucleotides, and membranes, made up of lipids)."
- "This subject is of great interest to biologists because macromolecules carry out most of the functions of cells, and it is only by coiling into specific three-dimensional shapes that they are able to perform these functions."
- "This architecture, the 'tertiary structure' of molecules, depends in a complicated way on each molecule's basic composition, or 'primary structure.'"
- "At lower resolutions, tools such as FIB-SEM tomography have allowed for a greater understanding of cells and their organelles in 3-dimensions."
- "In the past few years, it has also become possible to predict highly accurate physical molecular models to complement the experimental study of biological structures."
- "Computational techniques such as molecular dynamics simulations can be used in conjunction with empirical structure determination strategies to extend and study protein structure, conformation, and function."
- "How alterations in their structures affect their function."
- "How each hierarchical level of various extracellular matrices contributes to function (for example in bone)."
- "Early structural biologists throughout the 19th and early 20th centuries were primarily only able to study structures to the limit of the naked eye's visual acuity."
- "Now scientists could obtain the three-dimensional structures of biological molecules in atomic detail."
- "NMR spectroscopy allowed information about protein structure and dynamics to be obtained."
- "The development of more coherent electron sources, aberration correction for electron microscopes, and reconstruction software enabled the successful implementation of high-resolution cryo-electron microscopy."
- "Computational techniques such as molecular dynamics simulations can be used in conjunction with empirical structure determination strategies to extend and study protein structure, conformation, and function."