[{"data":1,"prerenderedAt":-1},["ShallowReactive",2],{"detail-sidebar-cat-0-en-105":3,"doc-seo-201717-105":59,"doc-detail-201717-en":130},{"code":4,"msg":5,"data":6},0,"success",[7,13,18,23,28,33,38,43,48,51,55],{"id":8,"doc_module":4,"doc_module_name":9,"category_name":10,"show_sort_weight":11,"slug":12},1,"Document","Story & Novel",90,"story-novel",{"id":14,"doc_module":4,"doc_module_name":9,"category_name":15,"show_sort_weight":16,"slug":17},2,"Literature",80,"literature",{"id":19,"doc_module":4,"doc_module_name":9,"category_name":20,"show_sort_weight":21,"slug":22},4,"Exam",70,"exam",{"id":24,"doc_module":4,"doc_module_name":9,"category_name":25,"show_sort_weight":26,"slug":27},5,"Comic",60,"comic",{"id":29,"doc_module":4,"doc_module_name":9,"category_name":30,"show_sort_weight":31,"slug":32},6,"Technology",50,"technology",{"id":34,"doc_module":4,"doc_module_name":9,"category_name":35,"show_sort_weight":36,"slug":37},7,"Healthcare",40,"healthcare",{"id":39,"doc_module":4,"doc_module_name":9,"category_name":40,"show_sort_weight":41,"slug":42},8,"Research & Report",30,"research-report",{"id":44,"doc_module":4,"doc_module_name":9,"category_name":45,"show_sort_weight":46,"slug":47},9,"Religion & Spirituality",20,"religion-spirituality",{"id":46,"doc_module":4,"doc_module_name":9,"category_name":49,"show_sort_weight":46,"slug":50},"World Cup","world-cup",{"id":52,"doc_module":4,"doc_module_name":9,"category_name":53,"show_sort_weight":52,"slug":54},10,"Lifestyle","lifestyle",{"id":56,"doc_module":4,"doc_module_name":9,"category_name":57,"show_sort_weight":24,"slug":58},19,"General","general",{"code":4,"msg":60,"data":61},"ok",{"site_id":62,"language":63,"slug":64,"title":65,"keywords":66,"description":67,"schema_data":68,"social_meta":123,"head_meta":125,"extra_data":127,"updated_unix":129},105,"en","high-yields-protein-structure","High Yields - Protein Structure","","Notes on protein structure focus on how the amino acid sequence determines folding and how peptide bonds form via condensation reactions. It explains peptide bond planarity from partial double-bond character, cis/trans configurations, and steric effects such as proline’s “kink.” The document then covers secondary structures (alpha helix, beta sheets, turns) stabilized by hydrogen bonds, followed by tertiary and quaternary organization, including globular protein features, domains, and major stabilizing forces like hydrophobic, ionic, van der Waals, and disulfide bridges.",{"@graph":69,"@context":122},[70,84,105],{"@type":71,"itemListElement":72},"BreadcrumbList",[73,77,79,82],{"item":74,"name":75,"@type":76,"position":8},"https://docshare.wps.com","Home","ListItem",{"item":78,"name":9,"@type":76,"position":14},"https://docshare.wps.com/document/",{"item":80,"name":35,"@type":76,"position":81},"https://docshare.wps.com/document/healthcare/",3,{"item":83,"name":65,"@type":76,"position":19},"https://docshare.wps.com/document/high-yields-protein-structure/201717/",{"url":83,"name":65,"@type":85,"image":86,"author":91,"headline":65,"publisher":94,"fileFormat":97,"inLanguage":63,"description":67,"dateModified":98,"datePublished":99,"encodingFormat":97,"isAccessibleForFree":100,"interactionStatistic":101},"DigitalDocument",{"url":87,"@type":88,"width":89,"height":90},"https://docshare.wps.com/thumbnails/high-yields-protein-structure/201717.png","ImageObject",300,407,{"name":92,"@type":93},"Taylor Morgan","Person",{"url":74,"name":95,"@type":96},"DocShare","Organization","application/pdf","2026-09-20","2026-09-04",true,{"@type":102,"interactionType":103,"userInteractionCount":81},"InteractionCounter",{"@type":104},"ViewAction",{"@type":106,"mainEntity":107},"FAQPage",[108,114,118],{"name":109,"@type":110,"acceptedAnswer":111},"How does the primary structure determine protein folding?","Question",{"text":112,"@type":113},"The primary structure is the amino acid sequence, and the document states that folding information is contained within it. The amino acid sequence must be correct for the protein to fold properly.","Answer",{"name":115,"@type":110,"acceptedAnswer":116},"Why is there no free rotation around the peptide bond?",{"text":117,"@type":113},"The peptide bond has partial double-bond character in equilibrium, making the peptide unit planar and rigid. Rotation is only possible around bonds to the alpha-carbons.",{"name":119,"@type":110,"acceptedAnswer":120},"What stabilizes secondary and tertiary protein structures?",{"text":121,"@type":113},"Secondary structures are stabilized by hydrogen bonds within the polypeptide backbone. Tertiary structure stabilization includes hydrogen bonds, hydrophobic interactions, van der Waals interactions, ionic bonds, and disulfide bridges.","https://schema.org",{"og:url":83,"og:type":124,"og:title":65,"og:site_name":95,"og:description":67},"article",{"robots":126,"canonical":83},"index,follow",{"doc_id":128,"site_id":62},201717,1788537619,{"code":4,"msg":5,"data":131},{"doc_id":128,"user_id":132,"nickname":92,"user_avatar":133,"doc_module":4,"category_id":34,"category_name":35,"doc_title":65,"doc_description":67,"doc_content":134,"file_id":135,"file_url":136,"file_type":137,"file_size":138,"view_count":81,"is_deleted":4,"is_public":8,"is_downloadable":8,"audit_status":8,"page_count":44,"language":139,"language_code":63,"site_id":62,"html_lang":63,"table_of_contents":140,"faqs":141,"seo_title":142,"seo_description":67,"update_tm":129,"read_time":143},1099523885336,"https://ap-avatar.wpscdn.com/davatar_276721f389ce27ea32af1340a28f341c","High yields* – protein structure  \n*These are not high yields from any teachers. This is what StudyAid finds relevant based on experience  \nPrimary structure  \n-­‐ Primary structure = amino acid sequence  \n-­‐ How to read an amino acid sequence:  \no from Amino (NH3) terminal 􀀡 to carboxyl terminal (how to remember it: A is the first letter in the alphabet)  \n-­‐ It is the amino acid sequence that decides how the protein is eventually going to fold  \n􀀡 all info about protein folding is in the primary structure  \n􀀡 amino acid sequence need to be correct for the protein to fold correctly  \n-­‐ Bonds: PEPTIDE BONDS  \nThe peptide bond:  \n-­‐  The peptide bond formation:  \no Two amino acids form a dipeptide through a CONDENSATION REACTION  \no Condensation reaction:  \n􀀢 two molecules are ”brought together” to form something more ”dense”, by loosing a small molecule  \n􀀢 Often the small molecule is WATER  \n-­‐  The partial double bond character of the peptide bond:  \no At any given time, 40% of the bonds will be double  \no The peptide bond is in an equilibrium, as shown on the picture below. It is this equilibrium that makes the double bond only partial.  \n􀀢 N donates an electron pair to carbonyl C  \n􀀢 The electrones are ”pushed” from C to O  \n􀀢 This forms an oxygen anion  \no The partial double bond makes sure there is NO FREE ROTATION AROUND THE PEPTIDE BOND (because there is never rotation around double bonds)  \no Length of the peptide bond: ca. 1,33 Å (longer than a double bond, shorter than a single bond)  \n-­‐  Cis and trans configurations:  \no The alpha-­‐carbons ofthe peptide bond can exist in a cis or trans configuration, as seen on the picture below  \n􀀢 Trans: the alpha-­‐carbons on either side of the peptide bond  \n􀀢 Cis: the alpha-­‐carbons on the same side of the peptide bond  \no The most common configuration: TRANS  \n􀀢 Why?  \n• Less steric hindrance between R1 and R2 (connected to the alpha-­‐carbons)  \no EXCEPTION: Proline  \n􀀢 Why?  \n• The N in proline is a part of a rigid ring, which limits its flexibility and rotation ability (alpha C-­‐N rotation is imposible)  \n• Proline gets a “kink” configuration in a polypeptide chain  \no Steric hindrance:  \n􀀢 Occur when molecules takes up space so that reactions gets hindered  \n􀀢 Steric means: happening in 3 dimensions  \n􀀢 Hindrance: hindering reactions  \n􀀢 The bigger the molecule is 􀀡 the less space  \n􀀢 Here is a link to a Khan Akademy movie giving an example on steric hindrance:  \n[https://](https://)www.khanacademy.org/science/organic-­‐chemistry/substitutionelimination-­‐reactions/sn1-­‐sn2-­‐sal/v/steric-­‐hindrance-­‐1  \n-­‐  Rotation:  \no No rotation about the partially double peptide bond  \n􀀢 Makes the peptide unit planar and rigid  \no Where can rotation occur?  \n􀀢 ONLY ABOUT THE BONDS TO THE ALPHA-­‐CARBONS  \n• Alpha C – C  \n• Alpha C – N  \no This also assure smaller steric hindrance  \nSecondary structure  \n-­‐ The backbone of a protein/ the polypeptide backbone: the linked polypeptide units (see the previous picture)  \no Rigid  \no Planar  \n-­‐ Major classes of secondary structures:  \no Alpha helix  \no Beta sheet  \no Beta turns  \n􀀢 These are ALL stabilized by HYDROGEN BONDS within the polypeptide backbone  \n! Hydrogen bonds: Hydrogen can form hydrogen bonds with:  \n1. Nitrogen  \n2. Oxygen  \n3. Fluorine  \n-­‐ Alpha helix:  \no Right handed helix (!Note the difference between alpha helix and collagen tripple helix, which is left handed!)  \no 3,6 residues pr turn  \no The side chains (R-­‐groups) project OUTWARDS  \no Bonds: HYDROGEN BONDS  \n􀀢 From C=O to H–N  \n􀀢 The hydrogen bonds are parallell to the helix  \no ! Proline!  \n􀀢 Is an ”Alpha helix breaker”(recall that proline causes a ”kink”in the polypeptide, due to its integrated Nitrogen in a rigid ring)  \n􀀢 Proline is therefore not common in alpha helices  \n-­‐  Beta sheets:  \no Composed of beta strands  \n􀀢 Parallel strands  \n􀀢 Antiparallel strands  \no Side chains: on both sides of the sheet (”under and over”)  \no Bonds and c","cbCaisc7dF8ljwEl","https://ap.wps.com/l/cbCaisc7dF8ljwEl","pdf",809275,"English","# Protein structure overview\n## Primary structure and peptide bonds\n## Secondary structure\n## Tertiary structure\n## Quaternary structure","[{\"question\":\"How does the primary structure determine protein folding?\",\"answer\":\"The primary structure is the amino acid sequence, and the document states that folding information is contained within it. The amino acid sequence must be correct for the protein to fold properly.\"},{\"question\":\"Why is there no free rotation around the peptide bond?\",\"answer\":\"The peptide bond has partial double-bond character in equilibrium, making the peptide unit planar and rigid. Rotation is only possible around bonds to the alpha-carbons.\"},{\"question\":\"What stabilizes secondary and tertiary protein structures?\",\"answer\":\"Secondary structures are stabilized by hydrogen bonds within the polypeptide backbone. Tertiary structure stabilization includes hydrogen bonds, hydrophobic interactions, van der Waals interactions, ionic bonds, and disulfide bridges.\"}]","High Yields - Protein Structure | PDF",23]