Editing Structural biology (section)

== History ==
In 1912 [[Max Von Laue]] directed X-rays at crystallized [[copper sulfate]] generating a [[Diffraction|diffraction pattern]].<ref>{{cite journal | vauthors = Curry S | title = Structural Biology: A Century-long Journey into an Unseen World | journal = Interdisciplinary Science Reviews | volume = 40 | issue = 3 | pages = 308–328 | date = July 2015 | pmid = 26740732 | pmc = 4697198 | doi = 10.1179/0308018815z.000000000120 | bibcode = 2015ISRv...40..308C | doi-access = free }}</ref> These experiments led to the development of [[X-ray crystallography]], and its usage in exploring biological structures.<ref name="Stoddart">{{Cite journal |last1=Jumper |first1=John |last2=Evans |first2=Richard |last3=Pritzel |first3=Alexander |last4=Green |first4=Tim |last5=Figurnov |first5=Michael |last6=Ronneberger |first6=Olaf |last7=Tunyasuvunakool |first7=Kathryn |last8=Bates |first8=Russ |last9=Žídek |first9=Augustin |last10=Potapenko |first10=Anna |last11=Bridgland |first11=Alex |last12=Meyer |first12=Clemens |last13=Kohl |first13=Simon A. A. |last14=Ballard |first14=Andrew J. |last15=Cowie |first15=Andrew |date=2021-07-15 |title=Highly accurate protein structure prediction with AlphaFold |journal=Nature |language=en |volume=596 |issue=7873 |pages=583–589 |doi=10.1038/s41586-021-03819-2 |pmid=34265844 |pmc=8371605 |bibcode=2021Natur.596..583J |issn=1476-4687}}</ref> In 1951, [[Rosalind Franklin]] and [[Maurice Wilkins]] used X-ray diffraction patterns to capture the first image of deoxyribonucleic acid (DNA). [[Francis Crick]] and [[James Watson]] modeled the double helical structure of DNA using this same technique in 1953 and received the Nobel Prize in Medicine along with Wilkins in 1962.<ref>{{Cite web |title=The Nobel Prize in Physiology or Medicine 1962 |url=https://www.nobelprize.org/prizes/medicine/1962/summary/ |access-date=2022-10-01 |website=NobelPrize.org |language=en-US}}</ref>

[[Pepsin]] crystals were the first proteins to be crystallized for use in X-ray diffraction, by [[Theodor Svedberg|Theodore Svedberg]] who received the 1962 Nobel Prize in Chemistry.<ref>{{cite journal | vauthors = Jaskolski M, Dauter Z, Wlodawer A | title = A brief history of macromolecular crystallography, illustrated by a family tree and its Nobel fruits | journal = The FEBS Journal | volume = 281 | issue = 18 | pages = 3985–4009 | date = September 2014 | pmid = 24698025 | pmc = 6309182 | doi = 10.1111/febs.12796 }}</ref> The first [[Protein tertiary structure|tertiary protein structure]], that of [[myoglobin]], was published in 1958 by [[John Kendrew]].<ref>{{cite journal | vauthors = Kendrew JC, Bodo G, Dintzis HM, Parrish RG, Wyckoff H, Phillips DC | title = A three-dimensional model of the myoglobin molecule obtained by x-ray analysis | journal = Nature | volume = 181 | issue = 4610 | pages = 662–666 | date = March 1958 | pmid = 13517261 | doi = 10.1038/181662a0 | bibcode = 1958Natur.181..662K | s2cid = 4162786 }}</ref> During this time, modeling of protein structures was done using [[Ochroma|balsa wood]] or [[wire]] models.<ref>{{cite journal | vauthors = Garman EF | title = Developments in x-ray crystallographic structure determination of biological macromolecules | journal = Science | volume = 343 | issue = 6175 | pages = 1102–1108 | date = March 2014 | pmid = 24604194 | doi = 10.1126/science.1247829 | bibcode = 2014Sci...343.1102G | s2cid = 21067016 }}</ref> With the invention of modeling software such as [[Collaborative Computational Project Number 4|CCP4]] in the late 1970s,<ref>{{Cite web|title=About CCP4|url=http://legacy.ccp4.ac.uk/about.php|access-date=2021-04-02|website=legacy.ccp4.ac.uk}}</ref> modeling is now done with computer assistance. Recent developments in the field have included the generation of [[Free-electron laser|X-ray free electron lasers]], allowing analysis of the dynamics and motion of biological molecules,<ref>{{cite journal | vauthors = Waldrop MM | title = X-ray science: The big guns | journal = Nature | volume = 505 | issue = 7485 | pages = 604–606 | date = January 2014 | pmid = 24476872 | doi = 10.1038/505604a | bibcode = 2014Natur.505..604W | doi-access = free }}</ref> and the use of structural biology in assisting [[synthetic biology]].<ref>{{cite journal | vauthors = Kiel C, Serrano L | title = Structural data in synthetic biology approaches for studying general design principles of cellular signaling networks | language = English | journal = Structure | volume = 20 | issue = 11 | pages = 1806–1813 | date = November 2012 | pmid = 23141693 | doi = 10.1016/j.str.2012.10.002 | doi-access = free | hdl = 10230/23121 | hdl-access = free }}</ref>

In the late 1930s and early 1940s, the combination of work done by [[Isidor Rabi]], [[Felix Bloch]], and [[Edward Mills Purcell]] led to the development of nuclear magnetic resonance (NMR). Currently, [[Solid-state nuclear magnetic resonance#:~:text=Solid-state NMR (ssNMR),magnetic resonance (NMR) spectroscopy.|solid-state NMR]] is widely used in the field of structural biology to determine the structure and dynamic nature of proteins ([[Nuclear magnetic resonance spectroscopy of proteins|protein NMR]]).<ref>{{cite journal | vauthors = Wüthrich K | title = The way to NMR structures of proteins | journal = Nature Structural Biology | volume = 8 | issue = 11 | pages = 923–925 | date = November 2001 | pmid = 11685234 | doi = 10.1038/nsb1101-923 | s2cid = 26153265 }}</ref>

In 1990, Richard Henderson produced the first three-dimensional, high resolution image of bacteriorhodopsin using [[cryogenic electron microscopy]] (cryo-EM).<ref>{{cite journal | vauthors = Henderson R, Baldwin JM, Ceska TA, Zemlin F, Beckmann E, Downing KH | title = Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy | journal = Journal of Molecular Biology | volume = 213 | issue = 4 | pages = 899–929 | date = June 1990 | pmid = 2359127 | doi = 10.1016/S0022-2836(05)80271-2 }}</ref> Since then, cryo-EM has emerged as an increasingly popular technique to determine three-dimensional, high resolution structures of biological images.<ref>{{Cite journal |last=Callaway |first=Ewen |date=2020-02-10 |title=Revolutionary cryo-EM is taking over structural biology |journal=Nature |language=en |volume=578 |issue=7794 |pages=201 |doi=10.1038/d41586-020-00341-9|pmid=32047310 |bibcode=2020Natur.578..201C |s2cid=211081167 |doi-access=free }}</ref>

More recently, computational methods have been developed to model and study biological structures. For example, [[molecular dynamics]] (MD) is commonly used to analyze the dynamic movements of biological molecules. In 1975, the first simulation of a biological folding process using MD was published in Nature.<ref>{{cite journal | vauthors = Levitt M, Warshel A | title = Computer simulation of protein folding | journal = Nature | volume = 253 | issue = 5494 | pages = 694–698 | date = February 1975 | pmid = 1167625 | doi = 10.1038/253694a0 | bibcode = 1975Natur.253..694L | s2cid = 4211714 }}</ref> Recently, [[Protein structure prediction#:~:text=Protein structure prediction is the,inverse problem of protein design.|protein structure prediction]] was significantly improved by a new machine learning method called [[AlphaFold]].<ref>{{cite journal | vauthors = Jumper J, Evans R, Pritzel A, Green T, Figurnov M, Ronneberger O, Tunyasuvunakool K, Bates R, Žídek A, Potapenko A, Bridgland A, Meyer C, Kohl SA, Ballard AJ, Cowie A, Romera-Paredes B, Nikolov S, Jain R, Adler J, Back T, Petersen S, Reiman D, Clancy E, Zielinski M, Steinegger M, Pacholska M, Berghammer T, Bodenstein S, Silver D, Vinyals O, Senior AW, Kavukcuoglu K, Kohli P, Hassabis D | display-authors = 6 | title = Highly accurate protein structure prediction with AlphaFold | journal = Nature | volume = 596 | issue = 7873 | pages = 583–589 | date = August 2021 | pmid = 34265844 | pmc = 8371605 | doi = 10.1038/s41586-021-03819-2 | bibcode = 2021Natur.596..583J }}</ref> Some claim that computational approaches are starting to lead the field of structural biology research.<ref>{{Cite journal|last1=Nussinov|first1=Ruth|last2=Tsai|first2=Chung-Jung|last3=Shehu|first3=Amarda|last4=Jang|first4=Hyunbum|date=2019-02-12|title=Computational Structural Biology: Successes, Future Directions, and Challenges|journal=Molecules (Basel, Switzerland)|volume=24|issue=3|pages=E637|doi=10.3390/molecules24030637|issn=1420-3049|pmc=6384756|pmid=30759724|doi-access=free}}</ref>