{"id":23,"date":"2019-06-22T12:25:19","date_gmt":"2019-06-22T02:25:19","guid":{"rendered":"https:\/\/protein.physics.unsw.edu.au\/?page_id=23"},"modified":"2019-07-04T15:04:22","modified_gmt":"2019-07-04T05:04:22","slug":"research","status":"publish","type":"page","link":"https:\/\/www.protein.physics.unsw.edu.au\/?page_id=23","title":{"rendered":"Continuing Research"},"content":{"rendered":"\n<h1 class=\"wp-block-heading\">Archaea &amp; Cold Adaptation<\/h1>\n\n\n\n<div style=\"height:100px\" aria-hidden=\"true\" class=\"wp-block-spacer\"><\/div>\n\n\n<p>Most of the biosphere (&gt;80%) is cold (permanently below 5\u00b0C), thus, a large proportion of organisms have evolved to thrive in cold environments. We are collaborating with\u00a0Rick Cavicchioli\u00a0(UNSW), who has established a comprehensive program to determine the mechanisms by which archaea adapts to cold environments. We are looking at factors that allow proteins to function at low temperature as well as molecular chaperones and protein folding in psychrophiles.\u00a0 We have determined the crystal structure of a monomeric form of the archaeal chaperonin, Cpn60, from the Antarctic psychrophile\u00a0Methanococcoides burtonii.\u00a0 We have discovered that nucleic acid binding proteins play an important role in stabilising nucleic acids at low temperatures.<\/p>\n<p>\u200b\u200b<strong>RNPs\u200b\u200b\u200b\u200b<\/strong><\/p>\n<p>Ribonucleoprotein complexes form some of the most ancient, central machines in extant organisms. The Sm\/Lsm proteins from a core ring structure that appears in many RNPs in all three domains of life.\u00a0In collaboration with\u00a0Bridget Mabbutt\u00a0(Macquarie University), we are using X-ray crystallography to gain a better understanding of these ring complexes in both archaea and eukarya.<\/p>\n\n\n<div style=\"height:100px\" aria-hidden=\"true\" class=\"wp-block-spacer\"><\/div>\n\n\n\n<ul class=\"wp-block-gallery columns-2 is-cropped wp-block-gallery-1 is-layout-flex wp-block-gallery-is-layout-flex\"><li class=\"blocks-gallery-item\"><figure><img loading=\"lazy\" decoding=\"async\" width=\"1024\" height=\"473\" src=\"https:\/\/protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/1N9R-Yeast-SmF-1024x473.png\" alt=\"\" data-id=\"60\" data-link=\"https:\/\/protein.physics.unsw.edu.au\/?attachment_id=60\" class=\"wp-image-60\" srcset=\"https:\/\/www.protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/1N9R-Yeast-SmF-1024x473.png 1024w, https:\/\/www.protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/1N9R-Yeast-SmF-300x139.png 300w, https:\/\/www.protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/1N9R-Yeast-SmF-768x355.png 768w, https:\/\/www.protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/1N9R-Yeast-SmF.png 1463w\" sizes=\"auto, (max-width: 1024px) 100vw, 1024px\" \/><figcaption>1N9R-Yeast-SmF<\/figcaption><\/figure><\/li><li class=\"blocks-gallery-item\"><figure><img loading=\"lazy\" decoding=\"async\" width=\"1024\" height=\"521\" src=\"https:\/\/protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/3AQ1-M.-Burtonii-GII-Gaperonin-1024x521.png\" alt=\"\" data-id=\"64\" data-link=\"https:\/\/protein.physics.unsw.edu.au\/?attachment_id=64\" class=\"wp-image-64\" srcset=\"https:\/\/www.protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/3AQ1-M.-Burtonii-GII-Gaperonin-1024x521.png 1024w, https:\/\/www.protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/3AQ1-M.-Burtonii-GII-Gaperonin-300x153.png 300w, https:\/\/www.protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/3AQ1-M.-Burtonii-GII-Gaperonin-768x391.png 768w, https:\/\/www.protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/3AQ1-M.-Burtonii-GII-Gaperonin.png 1499w\" sizes=\"auto, (max-width: 1024px) 100vw, 1024px\" \/><figcaption>3AQ1-M.-Burtonii-GII-Chaperonin<\/figcaption><\/figure><\/li><\/ul>\n\n\n\n<hr class=\"wp-block-separator is-style-wide\"\/>\n\n\n\n<div style=\"height:100px\" aria-hidden=\"true\" class=\"wp-block-spacer\"><\/div>\n\n\n\n<h1 class=\"wp-block-heading\"> Molecular Chaperones <\/h1>\n\n\n\n<div style=\"height:100px\" aria-hidden=\"true\" class=\"wp-block-spacer\"><\/div>\n\n\n<p>Protein folding is a key biological problem.\u00a0The environment in the cell is crowded and the conditions not necessarily conducive to spontaneous folding.\u00a0Several families of proteins are involved in assisting proteins to fold correctly or preventing aggregation and inappropriate interactions.\u00a0These proteins are known as molecular chaperones. We are focusing on several types of molecular chaperone, including the chaperonin, Cpn10.\u00a0Cpn10 also acts as an immunomodulatory protein and we are studying its structure in collaboration with\u00a0CBio Ltd Biopharmaceuticals,\u00a0Stephen Mahler\u00a0(University of Queensland)\u00a0and\u00a0Chris Marquis\u00a0(UNSW). We have also determined the crystal structure of a monomeric form of the archaeal chaperonin, Cpn60, from the Antarctic psychrophile\u00a0Methanococcoides burtonii\u00a0in collaboration with\u00a0Rick Cavicchioli\u00a0(UNSW).<\/p>\n\n\n<div style=\"height:100px\" aria-hidden=\"true\" class=\"wp-block-spacer\"><\/div>\n\n\n\n<ul class=\"wp-block-gallery columns-1 is-cropped wp-block-gallery-2 is-layout-flex wp-block-gallery-is-layout-flex\"><li class=\"blocks-gallery-item\"><figure><img loading=\"lazy\" decoding=\"async\" width=\"1024\" height=\"521\" src=\"https:\/\/protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/3AQ1-M.-Burtonii-GII-Gaperonin-1024x521.png\" alt=\"\" data-id=\"64\" data-link=\"https:\/\/protein.physics.unsw.edu.au\/?attachment_id=64\" class=\"wp-image-64\" srcset=\"https:\/\/www.protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/3AQ1-M.-Burtonii-GII-Gaperonin-1024x521.png 1024w, https:\/\/www.protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/3AQ1-M.-Burtonii-GII-Gaperonin-300x153.png 300w, https:\/\/www.protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/3AQ1-M.-Burtonii-GII-Gaperonin-768x391.png 768w, https:\/\/www.protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/3AQ1-M.-Burtonii-GII-Gaperonin.png 1499w\" sizes=\"auto, (max-width: 1024px) 100vw, 1024px\" \/><figcaption>3AQ1-M.-Burtonii-GII-Chaperonin<\/figcaption><\/figure><\/li><\/ul>\n\n\n\n<hr class=\"wp-block-separator is-style-wide\"\/>\n\n\n\n<div style=\"height:100px\" aria-hidden=\"true\" class=\"wp-block-spacer\"><\/div>\n\n\n\n<h1 class=\"wp-block-heading\">Integrons and Gene Cassette Proteins<\/h1>\n\n\n\n<div style=\"height:100px\" aria-hidden=\"true\" class=\"wp-block-spacer\"><\/div>\n\n\n<p>Lateral Gene transfer is a major phenomenon in bacteria and archaea.\u00a0The integron\/gene cassette system interconnects bacterial communities via a metagenome of cassette-encoded genes, which can be acquired, rearranged and discarded as a result of environmental pressure. The integron\/gene cassette system is the major mechanism by which pathogens gain antibiotic resistance.\u00a0Most of the proteins encoded by the gene cassettes are unrelated to proteins in the databases. We are exploring the function of these cassette proteins from environmental samples as well as\u00a0Vibrio, where many species contain large cassette arrays (&gt;100 genes). This is a collaboration with\u00a0Bridget Mabbutt\u00a0(Macquarie University) and Hatch Stokes (University of Technology Sydney).<\/p>\n\n\n<div style=\"height:100px\" aria-hidden=\"true\" class=\"wp-block-spacer\"><\/div>\n\n\n\n<ul class=\"wp-block-gallery columns-3 is-cropped wp-block-gallery-3 is-layout-flex wp-block-gallery-is-layout-flex\"><li class=\"blocks-gallery-item\"><figure><img loading=\"lazy\" decoding=\"async\" width=\"1024\" height=\"512\" src=\"https:\/\/protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/3IMO-Gene-Casette-protein-Cass14-Vibrio-1024x512.png\" alt=\"\" data-id=\"68\" data-link=\"https:\/\/protein.physics.unsw.edu.au\/?attachment_id=68\" class=\"wp-image-68\" srcset=\"https:\/\/www.protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/3IMO-Gene-Casette-protein-Cass14-Vibrio-1024x512.png 1024w, https:\/\/www.protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/3IMO-Gene-Casette-protein-Cass14-Vibrio-300x150.png 300w, https:\/\/www.protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/3IMO-Gene-Casette-protein-Cass14-Vibrio-768x384.png 768w, https:\/\/www.protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/3IMO-Gene-Casette-protein-Cass14-Vibrio.png 1513w\" sizes=\"auto, (max-width: 1024px) 100vw, 1024px\" \/><figcaption>3IMO-Gene Casette protein Cass14 Vibrio Cholerae<\/figcaption><\/figure><\/li><li class=\"blocks-gallery-item\"><figure><img loading=\"lazy\" decoding=\"async\" width=\"1024\" height=\"495\" src=\"https:\/\/protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/1TUH-Bal32a-Soil-Derived-Gene-Casette-1024x495.png\" alt=\"\" data-id=\"61\" data-link=\"https:\/\/protein.physics.unsw.edu.au\/?attachment_id=61\" class=\"wp-image-61\" srcset=\"https:\/\/www.protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/1TUH-Bal32a-Soil-Derived-Gene-Casette-1024x495.png 1024w, https:\/\/www.protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/1TUH-Bal32a-Soil-Derived-Gene-Casette-300x145.png 300w, https:\/\/www.protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/1TUH-Bal32a-Soil-Derived-Gene-Casette-768x371.png 768w, https:\/\/www.protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/1TUH-Bal32a-Soil-Derived-Gene-Casette.png 1493w\" sizes=\"auto, (max-width: 1024px) 100vw, 1024px\" \/><figcaption>1TUH-Bal32a-Soil-Derived-Gene-Casette<\/figcaption><\/figure><\/li><li class=\"blocks-gallery-item\"><figure><img loading=\"lazy\" decoding=\"async\" width=\"1024\" height=\"449\" src=\"https:\/\/protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/3I9s-Metagenome-Cholreae-Cass6-1024x449.png\" alt=\"\" data-id=\"66\" data-link=\"https:\/\/protein.physics.unsw.edu.au\/?attachment_id=66\" class=\"wp-image-66\" srcset=\"https:\/\/www.protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/3I9s-Metagenome-Cholreae-Cass6-1024x449.png 1024w, https:\/\/www.protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/3I9s-Metagenome-Cholreae-Cass6-300x131.png 300w, https:\/\/www.protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/3I9s-Metagenome-Cholreae-Cass6-768x337.png 768w, https:\/\/www.protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/3I9s-Metagenome-Cholreae-Cass6.png 1595w\" sizes=\"auto, (max-width: 1024px) 100vw, 1024px\" \/><figcaption> 3I9s-Metagenome-Cholreae-Cass6<\/figcaption><\/figure><\/li><li class=\"blocks-gallery-item\"><figure><img loading=\"lazy\" decoding=\"async\" width=\"1024\" height=\"531\" src=\"https:\/\/protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/3GHJ-Halifax-Harbour-Sewerage-Integraon-Casette-1024x531.png\" alt=\"\" data-id=\"65\" data-link=\"https:\/\/protein.physics.unsw.edu.au\/?attachment_id=65\" class=\"wp-image-65\" srcset=\"https:\/\/www.protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/3GHJ-Halifax-Harbour-Sewerage-Integraon-Casette-1024x531.png 1024w, https:\/\/www.protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/3GHJ-Halifax-Harbour-Sewerage-Integraon-Casette-300x156.png 300w, https:\/\/www.protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/3GHJ-Halifax-Harbour-Sewerage-Integraon-Casette-768x398.png 768w, https:\/\/www.protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/3GHJ-Halifax-Harbour-Sewerage-Integraon-Casette.png 1247w\" sizes=\"auto, (max-width: 1024px) 100vw, 1024px\" \/><figcaption>3GHJ-Halifax-Harbour-Sewerage-Integraon-Casette<\/figcaption><\/figure><\/li><li class=\"blocks-gallery-item\"><figure><img loading=\"lazy\" decoding=\"async\" width=\"1024\" height=\"502\" src=\"https:\/\/protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/3IF4-Sewerage-Northwest-arm-1024x502.png\" alt=\"\" data-id=\"67\" data-link=\"https:\/\/protein.physics.unsw.edu.au\/?attachment_id=67\" class=\"wp-image-67\" srcset=\"https:\/\/www.protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/3IF4-Sewerage-Northwest-arm-1024x502.png 1024w, https:\/\/www.protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/3IF4-Sewerage-Northwest-arm-300x147.png 300w, https:\/\/www.protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/3IF4-Sewerage-Northwest-arm-768x376.png 768w, https:\/\/www.protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/3IF4-Sewerage-Northwest-arm.png 1639w\" sizes=\"auto, (max-width: 1024px) 100vw, 1024px\" \/><figcaption>3IF4-Sewerage-Northwest-arm<\/figcaption><\/figure><\/li><\/ul>\n\n\n\n<hr class=\"wp-block-separator is-style-wide\"\/>\n\n\n\n<div style=\"height:100px\" aria-hidden=\"true\" class=\"wp-block-spacer\"><\/div>\n\n\n\n<h1 class=\"wp-block-heading\">Protease Inhibitors and Serpins<\/h1>\n\n\n\n<div style=\"height:100px\" aria-hidden=\"true\" class=\"wp-block-spacer\"><\/div>\n\n\n<p>The serpin family proteins are usually protease inhibitors. They are the most important regulators of proteases in eukaryotes. They work via a \u201cmouse trap\u201d mechanism whereby a target protease begins to cut the serpin \u201cbait\u201d (Reactive Centre Loop) and becomes covalently trapped and unfolded as the serpin moves from its metastable active state to its stable RCL inserted state. This structural change involves the insertion of the RCL into the centre of a \u03b2 sheet in the middle of the serpin.\u200b<\/p>\n<p><strong>Human Plasminogen Activator Inhibitor 2 (PAI-2)<em>\u200b<\/em><\/strong><\/p>\n<p>PAI-2 is a serpin that finds, binds to and inhibits plasminogen activators such as urokinase. During the process of inhibition, the serpin undergoes an incredible conformational change, which involves\u00a0inserting a loop into a beta sheet as an extra strand. We have determined the crystal structure of human PAI-2 in the active (stressed) state (<a href=\"http:\/\/www.imb-jena.de\/cgi-bin\/ImgLib.pl?CODE=1by7\" target=\"_blank\" rel=\"noreferrer noopener\">image<\/a>,\u00a0<a href=\"http:\/\/molmod.angis.org.au\/oca-bin\/ocashort?id=1by7\" target=\"_blank\" rel=\"noreferrer noopener\">PDB entry: 1BY7<\/a>) and relaxed state, where a peptide corresponding to the RCL has inserted into the central \u03b2 sheet. We have used our analysis of residue correlations in \u03b2 sheets to gain understanding of this process. We have determined several structures where the P8 site in the RCL has been mutated in the peptide and inserted into the \u03b2 sheet.\u200b<\/p>\n<p><strong>Arabidopsis serpin AtSerpin1<\/strong><em>\u200b<\/em><\/p>\n<p>Serpins are important regulatory proteins in plants. We have determined the first crystal structure of a plant serpin, AtSerpin1 from\u00a0Arabidopsis thaliana\u00a0in the active form. The structure shows several features that are unique to plant serpins. This is a collaboration with\u00a0<a href=\"http:\/\/sydney.edu.au\/agriculture\/academic_staff\/tom.roberts.php\" target=\"_blank\" rel=\"noreferrer noopener\">Tom Roberts<\/a>\u00a0(University of Sydney) and\u00a0<a href=\"http:\/\/www.weizmann.ac.il\/plants\/fluhr\/\" target=\"_blank\" rel=\"noreferrer noopener\">Robert Fluhr<\/a>\u00a0(Weizmann Institute).\u200b<\/p>\n<p><strong>Rubisco<\/strong><em>\u200b<\/em><\/p>\n<p>Rubisco is the most abundant protein in plants. Based on the structure, we have postulated a mechanism for closing and a mechanism for catalysis. (<a href=\"http:\/\/www.imb-jena.de\/cgi-bin\/ImgLib.pl?CODE=1ej7\" target=\"_blank\" rel=\"noreferrer noopener\">image<\/a>,\u00a0<a href=\"http:\/\/molmod.angis.org.au\/oca-bin\/ocashort?id=1EJ7\" target=\"_blank\" rel=\"noreferrer noopener\">PDB entry: 1EJ7<\/a>).<\/p>\n\n\n<div style=\"height:100px\" aria-hidden=\"true\" class=\"wp-block-spacer\"><\/div>\n\n\n\n<ul class=\"wp-block-gallery columns-3 is-cropped wp-block-gallery-4 is-layout-flex wp-block-gallery-is-layout-flex\"><li class=\"blocks-gallery-item\"><figure><img loading=\"lazy\" decoding=\"async\" width=\"1024\" height=\"508\" src=\"https:\/\/protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/4RUB-Rubisco-1024x508.png\" alt=\"\" data-id=\"79\" data-link=\"https:\/\/protein.physics.unsw.edu.au\/?attachment_id=79\" class=\"wp-image-79\" srcset=\"https:\/\/www.protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/4RUB-Rubisco-1024x508.png 1024w, https:\/\/www.protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/4RUB-Rubisco-300x149.png 300w, https:\/\/www.protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/4RUB-Rubisco-768x381.png 768w, https:\/\/www.protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/4RUB-Rubisco.png 1555w\" sizes=\"auto, (max-width: 1024px) 100vw, 1024px\" \/><figcaption>4RUB-Rubisco<\/figcaption><\/figure><\/li><li class=\"blocks-gallery-item\"><figure><img loading=\"lazy\" decoding=\"async\" width=\"1024\" height=\"486\" src=\"https:\/\/protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/2Arr-Plasminogen-inhibor-2-serpin-1024x486.png\" alt=\"\" data-id=\"63\" data-link=\"https:\/\/protein.physics.unsw.edu.au\/?attachment_id=63\" class=\"wp-image-63\" srcset=\"https:\/\/www.protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/2Arr-Plasminogen-inhibor-2-serpin-1024x486.png 1024w, https:\/\/www.protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/2Arr-Plasminogen-inhibor-2-serpin-300x142.png 300w, https:\/\/www.protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/2Arr-Plasminogen-inhibor-2-serpin-768x365.png 768w, https:\/\/www.protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/2Arr-Plasminogen-inhibor-2-serpin.png 1643w\" sizes=\"auto, (max-width: 1024px) 100vw, 1024px\" \/><figcaption>2Arr-Plasminogen-inhibor-2-serpin<\/figcaption><\/figure><\/li><li class=\"blocks-gallery-item\"><figure><img loading=\"lazy\" decoding=\"async\" width=\"1024\" height=\"527\" src=\"https:\/\/protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/3Le2-arabadopsin-serpin-stressed-conformation-1024x527.png\" alt=\"\" data-id=\"70\" data-link=\"https:\/\/protein.physics.unsw.edu.au\/?attachment_id=70\" class=\"wp-image-70\" srcset=\"https:\/\/www.protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/3Le2-arabadopsin-serpin-stressed-conformation-1024x527.png 1024w, https:\/\/www.protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/3Le2-arabadopsin-serpin-stressed-conformation-300x154.png 300w, https:\/\/www.protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/3Le2-arabadopsin-serpin-stressed-conformation-768x395.png 768w, https:\/\/www.protein.physics.unsw.edu.au\/wp-content\/uploads\/2019\/06\/3Le2-arabadopsin-serpin-stressed-conformation.png 1587w\" sizes=\"auto, (max-width: 1024px) 100vw, 1024px\" \/><figcaption>3Le2-arabadopsin-serpin-stressed-conformation<\/figcaption><\/figure><\/li><\/ul>\n\n\n\n<hr class=\"wp-block-separator is-style-wide\"\/>\n\n\n\n<div style=\"height:100px\" aria-hidden=\"true\" class=\"wp-block-spacer\"><\/div>\n\n\n\n<h1 class=\"wp-block-heading\"> \u03b2  Sheet Structures in Proteins<\/h1>\n\n\n\n<div style=\"height:100px\" aria-hidden=\"true\" class=\"wp-block-spacer\"><\/div>\n\n\n<p><strong>Why do particular segments of a protein form \u03b2 structures?\u200b<\/strong><\/p>\n<p>We have analysed the sequences of \u03b2 structures in proteins to gain a better understanding of their formation. In particular, we have discovered correlations between neighbouring residues across strands. These may be important in protein folding and the formation of amyloid.\u200b<\/p>\n<p><strong>What is the physical origin of twist &amp; shear in \u03b2 sheets and \u03b2 ribbons?<em>\u200b<\/em><\/strong><\/p>\n<p>We have analysed the correlations between physical properties of \u03b2 structures in proteins. Using this data, we have identified the physical mechanism responsible for the shear and twist of \u03b2 sheets.<\/p>","protected":false},"excerpt":{"rendered":"<p>Archaea &amp; Cold Adaptation Most of the biosphere (&gt;80%) is cold (permanently below 5\u00b0C), thus, a large proportion of organisms have evolved to thrive in cold environments. We are collaborating with\u00a0Rick Cavicchioli\u00a0(UNSW), who has established a comprehensive program to determine the mechanisms by which archaea adapts to cold environments. We are looking at factors that allow proteins to function at low temperature as well as molecular chaperones and protein folding<\/p>\n<div class=\"read-more\"><a class=\"btn read-more-btn\" href=\"https:\/\/www.protein.physics.unsw.edu.au\/?page_id=23\">Read More<\/a><\/div>\n","protected":false},"author":1,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"footnotes":""},"class_list":["post-23","page","type-page","status-publish","hentry"],"_links":{"self":[{"href":"https:\/\/www.protein.physics.unsw.edu.au\/index.php?rest_route=\/wp\/v2\/pages\/23","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/www.protein.physics.unsw.edu.au\/index.php?rest_route=\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/www.protein.physics.unsw.edu.au\/index.php?rest_route=\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/www.protein.physics.unsw.edu.au\/index.php?rest_route=\/wp\/v2\/users\/1"}],"replies":[{"embeddable":true,"href":"https:\/\/www.protein.physics.unsw.edu.au\/index.php?rest_route=%2Fwp%2Fv2%2Fcomments&post=23"}],"version-history":[{"count":45,"href":"https:\/\/www.protein.physics.unsw.edu.au\/index.php?rest_route=\/wp\/v2\/pages\/23\/revisions"}],"predecessor-version":[{"id":264,"href":"https:\/\/www.protein.physics.unsw.edu.au\/index.php?rest_route=\/wp\/v2\/pages\/23\/revisions\/264"}],"wp:attachment":[{"href":"https:\/\/www.protein.physics.unsw.edu.au\/index.php?rest_route=%2Fwp%2Fv2%2Fmedia&parent=23"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}