Editing Structural biology (section)

{{Short description|Study of molecular structures in biology}}
{{Biochemistry sidebar}}
'''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.<ref>{{cite book |last1=Liljas |first1=Anders |chapter=What is Structural Biology and When Did It Start |pages=7–9 |chapter-url={{GBurl|aCvtLB0hX44C|p=7}} |title=Textbook of Structural Biology |date=2009 |publisher=World Scientific |isbn=978-981-277-207-7 }}</ref> 

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. In the 20th century, a variety of experimental techniques were developed to examine the 3D structures of biological molecules. The most prominent techniques are [[X-ray crystallography]], [[nuclear magnetic resonance]], and [[Electron microscope|electron microscopy]]. Through the discovery of [[X-ray|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.<ref>{{cite journal |last1=Curry |first1=Stephen |title=Structural Biology: A Century-long Journey into an Unseen World |journal=Interdisciplinary Science Reviews |date=3 July 2015 |volume=40 |issue=3 |pages=308–328 |doi=10.1179/0308018815Z.000000000120 |pmc=4697198 |pmid=26740732 |bibcode=2015ISRv...40..308C }}</ref> Likewise, [[Nuclear magnetic resonance spectroscopy|NMR spectroscopy]] allowed information about protein structure and dynamics to be obtained.<ref>{{cite journal |last1=Campbell |first1=Iain D. |title=The evolution of protein NMR |journal=Biomedical Spectroscopy and Imaging |date=2013 |volume=2 |issue=4 |pages=245–264 |doi=10.3233/BSI-130055 |doi-access=free }}</ref> Finally, 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, thereby permitting the study of individual proteins and molecular complexes in three-dimensions at angstrom resolution.

With the development of these three techniques, the field of structural biology expanded and also became a branch of [[molecular biology]], [[biochemistry]], and [[biophysics]] concerned with the molecular structure of biological [[macromolecule]]s (especially [[protein]]s, made up of [[amino acid]]s, [[RNA]] or [[DNA]], made up of [[nucleotide]]s, and [[Biological membrane|membranes]], made up of [[lipid]]s), how they acquire the structures they have, and how alterations in their structures affect their function.<ref>{{cite book |last1=Banaszak |first1=Leonard J. |title=Foundations of Structural Biology |date=2000 |publisher=Elsevier |isbn=978-0-08-052184-8 }}{{pn|date=February 2025}}</ref> This subject is of great interest to biologists because macromolecules carry out most of the functions of [[cell (biology)|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 greater understanding of cells and their organelles in 3-dimensions, and how each hierarchical level of various extracellular matrices contributes to function (for example in bone). In the past few years it has also become possible to predict highly accurate physical [[molecular model]]s to complement the experimental study of biological structures.<ref name="Stoddart" /> 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.<ref>{{cite journal |last1=Karplus |first1=Martin |last2=McCammon |first2=J. Andrew |title=Molecular dynamics simulations of biomolecules |journal=Nature Structural Biology |date=September 2002 |volume=9 |issue=9 |pages=646–652 |doi=10.1038/nsb0902-646 |pmid=12198485 }}</ref>[[File:Hemoglobin t-r state ani.gif|thumb|[[Hemoglobin]], the oxygen transporting protein found in red blood cells]]

[[File:Protein structure examples.png|thumb|Examples of protein structures from the [[Protein Data Bank]] (PDB)|alt=]]