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tertiary structure of protein example

by Zachariah Metz Published 4 years ago Updated 2 years ago

Tertiary Structure Deals with the Three-Dimensional Arrangement of All of the Amino acids. The tertiary structure of proteins deals with how the regional structures are put together in space. For example, the α-helices may be oriented parallel to each other or at right angles.

Full Answer

Which best describes the tertiary structure of a protein?

Tertiary Structure

  • Tertiary Structure Interactions. The following are the main interactions that make up the tertiary structures of proteins. ...
  • Types of Tertiary Structures. Most proteins fall into this category. ...
  • Related Biology Terms. Cofactor – An essential non-protein component in enzymes that activates them or plays a role in the chemical reactions.
  • Quiz. ...

What is meant by a tertiary structure protein?

The tertiary structure of a protein consists of the way a polypeptide is formed of a complex molecular shape. This is caused by R-group interactions such as ionic and hydrogen bonds, disulphide bridges, and hydrophobic & hydrophilic interactions. Protein tertiary structure is the three dimensional shape of a protein.

What is the tertiary structure of a protein determined by?

The tertiary structure is the final specific geometric shape that a protein assumes. This final shape is determined by a variety of bonding interactions between the "side chains" on the amino acids. These bonding interactions may be stronger than the hydrogen bonds between amide groups holding the helical structure.

What is the primary level of a protein structure?

To understand how a protein gets its final shape or conformation, we need to understand the four levels of protein structure: primary, secondary, tertiary, and quaternary. The simplest level of protein structure, primary structure, is simply the sequence of amino acids in a polypeptide chain.

Is insulin a tertiary structure?

Tertiary structure The three-dimensional structure of insulin is further stabilised by disulphide bridges. These form between thiol groups (-SH) on cysteine residues (CYS above).

Is keratin a tertiary structure?

In fact, the association of α helices into coiled-coil structures like keratin is an example of quaternary structure, and the left-handed superhelical twist of this association gives keratin an extra measure of tensile strength appropriate for this fibrous, structural protein.

Is hemoglobin an example of tertiary structure of protein?

However, hemoglobin's quaternary structure sets it apart. The quaternary structure of a hemoglobin molecule includes four tertiary structure protein chains, which are all alpha helices. Individually, each alpha helix is a secondary polypeptide structure made of amino acid chains.

What are the 4 types of tertiary structure of proteins?

Protein tertiary structure is due to interactions between R groups in the protein. Note that these R groups MUST be facing each other to interact. There are four types of tertiary interactions: hydrophobic interactions, hydrogen bonds, salt bridges, and sulfur-sulfur covalent bonds.

Is hemoglobin A tertiary structure?

Hemoglobin. Hemoglobin has a quaternary structure. It consists of two pairs of different proteins, designated the α and β chains. There are 141 and 146 amino acids in the α and β chains of hemoglobin, respectively.

What is an example of tertiary structure?

Tertiary Structure Deals with the Three-Dimensional Arrangement of All of the Amino acids. The tertiary structure of proteins deals with how the regional structures are put together in space. For example, the α-helices may be oriented parallel to each other or at right angles.

Is myoglobin a tertiary structure?

The tertiary structure of myoglobin is that of a typical water-soluble globular protein. Its secondary structure is unusual in which it contains a very high proportion (75%) of α-helical secondary structure. Each myoglobin molecule contains a single heme group inserted into a hydrophobic cleft in the protein.

Is myoglobin a tertiary or quaternary structure?

Hemoglobin has a quaternary structure composed of two alpha and two beta subunits, whereas myoglobin has a tertiary structure.

Is alpha helix a tertiary structure?

An alpha helix is an element of secondary structure in which the amino acid chain is arranged in a spiral.

Are disulfide bonds tertiary structure?

Finally, there's one special type of covalent bond that can contribute to tertiary structure: the disulfide bond. Disulfide bonds, covalent linkages between the sulfur-containing side chains of cysteines, are much stronger than the other types of bonds that contribute to tertiary structure.

Is Collagen a secondary or tertiary structure?

All multicellular animals possess collagens as major structural proteins which are responsible for maintaining the structural integrity of tissues and organs. Collagens are characterized by their unique tertiary structure, called the collagen triple helix, and by their existence in extracellular matrices (ECMs).

What is an example of a secondary protein structure?

A secondary structure of a protein pertains to the folding of a polypeptide chain, resulting in an alpha helix, beta sheet or a random coil structure. Another example of a secondary structure is that of a nucleic acid such as the clover leaf structure of tRNA.

What are the four types of protein structures?

The four types of protein structure are: Primary - The amino acid sequence of a protein Secondary - The hydrogen-bonding pattern, usually either...

What bonds are in the tertiary structure of a protein?

The bonds in the tertiary structure of a protein involve disulfide bonds, hydrogen bonds, ionic bonds, and hydrophobic interactions. These bonds cr...

What are the functions of proteins?

The functions of proteins vary widely but can include: Structure Motility Cell division Enzymatic catalysts Transport Storage Adhesion Immu...

What is the tertiary structure of a protein?

Tertiary Structure. The tertiary structure of a protein refers to the arrangement of amino acid side chains in the protein. Generally, the information for protein structure is contained within the amino acid sequence of the protein itself. This important principle of biochemistry was first determined by the biochemist Christian Anfinsen in studies ...

Which amino acid is hydrophobic?

Conversely, the hydrophilic amino acids, such as glutamic acid, serine, or asparagine, ...

What happens when a protein folds?

When a protein folds, either as it is being made on ribosomes or refolded after it is purified, the first step involves the formation of hydrogen bonds within the structure to nucleate secondary structural (alpha and beta) regions. For example, amide hydrogen atoms can form H‐bonds with nearby carbonyl oxygens;

Where are hydrophilic amino acids found?

Conversely, the hydrophilic amino acids, such as glutamic acid, serine, or asparagine, are generally found on the outside surface of the protein, where they are available for interaction with water. Alternatively, when these groups are found on the inside of soluble proteins, they often form charge‐charge interactions, or salt bridges, ...

Do proteins help fold?

Proteins may assist the folding of other proteins. Although the native, active structure of a protein is thought to be the most stable one thermodynamically, it isn't always achieved in high yield when a protein is allowed to fold on its own.

What is the tertiary structure of a protein?

The tertiary structure of a protein consists of the way a polypeptide is formed of a complex molecular shape. This is caused by R-group interactions such as ionic and hydrogen bonds, disulphide bridges, and hydrophobic & hydrophilic interactions. Protein tertiary structure is the three dimensional shape of a protein.

What determines a protein's tertiary structure?

The interactions and bonds of side chains within a particular protein determine its tertiary structure. The protein tertiary structure is defined by its atomic coordinates. These coordinates may refer either to a protein domain or to the entire tertiary structure. A number of tertiary structures may fold into a quaternary structure.

Why are protein structures dynamic?

Because many similar conformations will have similar energies, protein structures are dynamic, fluctuating between a large these similar structures.

What is the most common tool used to determine protein structure?

X-ray crystallography is the most common tool used to determine protein structure. It provides high resolution of the structure but it does not give information about protein's conformational flexibility .

What is the structure of a protein that is bound to a ligand?

Ligand binding. The structure of a protein, for example an enzyme, may change upon binding of its natural ligands, for example a cofactor. In this case, the structure of the protein bound to the ligand is known as holo structure, of the unbound protein as apo structure.

What is the term for a protein that is folded into its native state?

Thermostability. See also: Equilibrium unfolding. A protein folded into its native state or native conformation typically has a lower Gibbs free energy (a combination of enthalpy and entropy) than the unfolded conformation. A protein will tend towards low-energy conformations, which will determine the protein's fold in the cellular environment.

How does protein structure prediction work?

Protein structure prediction is a new way to create disease models , which may avoid the use of animals.

What Is the Tertiary Structure of a Protein?

The tertiary structure of a protein is the three-dimensional conformation of a protein. Proteins are important aspects of all cellular structures and functions and play an important role in multicellular organisms as well. Proteins have functions such as the following:

Protein Structure Diagram

There are several levels of structure in proteins. The specific amino acid sequence is the primary structure. Amino acids are the monomers of protein, and there is twenty total in the body. All amino acids have a similar structure.

Protein Structure and Function

Why is the shape of a protein important? The shape of a protein is important because it allows proteins to carry out their functions in the body. Proteins have various functions, such as transporting materials across the cell membrane, catalyzing chemical reactions, regulating cell growth and division, and many others.

What forces drive tertiary structure?

Forces That Drive Tertiary Structure. Most proteins fold into their tertiary structure in an aqueous environment - a cell is, after all, 60% water. The chemical properties of the various R-groups (sidechains) of the amino acids within the protein chain will influence the way that the protein folds in its environment.

What is the final shape of a protein?

A protein needs to adopt a final and stable 3-dimensional shape in order to function properly. The Tertiary Structure of a protein is the arrangement of the secondary structures into this final 3-dimensional shape.

Why do proteins fold in the same shape?

This pattern is due to the properties of its unique sequence of amino acids (primary structure). As long as the sequence of amino acids is the same, the protein will fold into the same 3-dimensional shape.

Why is it important to study protein structure?

If a protein does not fold correctly it will not function properly. Therefore, researching a protein's structure is very important when trying to understand what it does and how it works. When scientists study a protein they must first determine the sequence of amino acids in the protein chain (primary structure).

Why are proteins so amazing?

Proteins are amazing molecules because they come in a huge variety of sizes and shapes; each shape suited to perform a specific task. The primary sequence of amino acids in a protein determines its 3-dimensional shape which, in turn, determines how the protein will function. This structure-function relationship is key to appreciating proteins ...

Where are hydrophobic amino acids located?

Hydrophilic amino acids will interact with the water molecules, and thus tend to be located on the outer surface of the protein. Basic (positvely charged) amino acids and Acidic (negatively charged) amino acids create salt bridges, ...

How do amino acids interact with water?

When a protein is surrounded by water: 1 Hydrophobic amino acids will move away from the water and bury themselves in the center of the protein. 2 Hydrophilic amino acids will interact with the water molecules, and thus tend to be located on the outer surface of the protein. 3 Basic (positvely charged) amino acids and Acidic (negatively charged) amino acids create salt bridges, or electrostatic interactions, to further stabilize the tertiary structure. 4 Cysteines may form a disulfide bridge, further stabilizing the protein.

What is the tertiary structure of a protein?

The tertiary structure of protein definition is the arrangement of amino acid side chains in the protein. Generally, the information for protein structure is contained within the amino acid sequence of the protein itself. This important principle of biochemistry was first determined by the biochemist “ Christian Anfinsen ” in studies ...

What is the final shape of a protein?

The tertiary structure is the final specific geometric shape that a protein assumes. This final shape is determined by a variety of bonding interactions between the “side chains” on the amino acids. These binding interactions may be stronger than the hydrogen bonds between amide groups holding the helical structure.

How many amino acids are in ribonuclease?

The native enzyme has 124 amino acids; 8 of these are cysteines, forming 4 disulfide bonds. When ribonuclease was treated with mercaptoethanol to destroy the disulfide bonds and urea to disrupt its secondary and tertiary structure of the protein, all enzymatic activity was lost.

Why avoid amyloid formation?

Avoidance of amyloid formation may account for the large investment in the cell in chaperones and proteasomes as well as the crucial importance of particular amino acid side chains in maintaining a globular , and hence soluble, tertiary structure.

What happens to a protein if it is disrupted?

The function of a protein (except as food) depends on its tertiary structure. If this is disrupted, the protein is said to be denatured, and it loses its activity. Examples: A mutation in the gene encoding a protein is a frequent cause of altered tertiary structure.

What is hydrophobic interaction?

Hydrophobic interaction definition is the relations between water and hydrophobes (low water-soluble molecules). Hydrophobes are nonpolar molecules and usually have a long chain of carbons that do not interact with water molecules. The mixing of fat and water is a good example of this particular interaction.

What is hydrogen bonding?

Hydrogen Bonding. Hydrogen bonding between “side chains” occurs in a variety of circumstances. The most usual cases are between two alcohols, an alcohol and an acid, two acids, or alcohol, and an amine or amide.

What are the four levels of protein structure?

To understand how a protein gets its final shape or conformation, we need to understand the four levels of protein structure: primary, secondary, tertiary, and quaternary.

How many levels of structure are there in proteins?

Many proteins are made up of a single polypeptide chain and have only three levels of structure (the ones we’ve just discussed). However, some proteins are made up of multiple polypeptide chains, also known as subunits. When these subunits come together, they give the protein its quaternary structure.

How are amino acids connected to each other?

They are connected to one another by disulfide bonds (sulfur-sulfur bonds between cysteines). The A chain also contains an internal disulfide bond. The amino acids that make up each chain of insulin are represented as connected circles, each with the three-letter abbreviation of the amino acid's name.

How many amino acids are in a hemoglobin molecule?

What is most remarkable to consider is that a hemoglobin molecule is made up of two α chains and two β chains, each consisting of about 150 amino acids, for a total of about 600 amino acids in the whole protein.

How many polypeptide chains are there in insulin?

For example, the hormone insulin has two polypeptide chains, A and B, shown in diagram below. (The insulin molecule shown here is cow insulin, although its structure is similar to that of human insulin.) Each chain has its own set of amino acids, assembled in a particular order.

Where do the R groups of amino acids stick outward?

The R groups of the amino acids stick outward from the α helix, where they are free to interact. In a β pleated sheet, two or more segments of a polypeptide chain line up next to each other, forming a sheet-like structure held together by hydrogen bonds.

Which amino acids have large ring structures in their R groups?

Similarly, amino acids such as tryptophan, tyrosine, and phenylalanine, which have large ring structures in their R groups, are often found in β pleated sheets, perhaps because the β pleated sheet structure provides plenty of space for the side chains.

How is a tertiary structure formed?

The tertiary structure of a protein is formed due to various interactions. These interactions allow protein molecules to twist and bend so that they can achieve their stable state. This stable form of the protein is called its native conformation. The native conformation of a protein is stabilized by four types of non-covalent interactions. These interactions are as follows:

What changes the primary sequence of proteins?

The alteration in the primary sequence of protein may take place due to ultraviolet radiation and by an error in DNA replication. This change will alter the primary sequence and disturb the native conformation of the tertiary structure.

How do different proteins affect their specificity?

The conformation or shape of the protein determines its specificity. Each protein has a unique sequence of the amino acids in its primary structure. Proteins that have the same sequence of amino acids will fold into the same 3-D shape to perform the same function. The change in the tertiary structure of a protein affects the function of the protein.

Tertiary Structure Definition

Image
The tertiary structure is the structure at which polypeptide chains become functional. At this level, every protein has a specific three-dimensional shape and presents functional groups on its outer surface, allowing it to interact with other molecules, and giving it its unique function. The arrangement is made with the hel…
See more on biologydictionary.net

Tertiary Structure Interactions

  • The following are the main interactions that make up the tertiary structures of proteins. They guide the bending and twisting that help the protein molecule achieve a stable state. We can observe interactions that are covalent, where pairs of electrons are shared between atoms, or non-covalent, where pairs of electrons are not shared between atoms. Recall that the breaking d…
See more on biologydictionary.net

Related Biology Terms

  1. Cofactor– An essential non-protein component in enzymes that activates them or plays a role in the chemical reactions.
  2. Isomer – Compounds with different arrangements of atoms but the same chemical formula.
  3. Ligand – A substance, such as a hormone, that binds to a specific biomolecule to serve a purpose.
  1. Cofactor– An essential non-protein component in enzymes that activates them or plays a role in the chemical reactions.
  2. Isomer – Compounds with different arrangements of atoms but the same chemical formula.
  3. Ligand – A substance, such as a hormone, that binds to a specific biomolecule to serve a purpose.
  4. Quaternary structure– Forms when a number of protein subunits cluster together into a complex.
See more on biologydictionary.net

Quiz

  • 1. Which of the following is not true of the tertiary structure? A. It is functional B. It contains three polypeptide chains C. It involves ionic bonds D.It involves hydrophobic interactions 2. Which of the following refers to the sequence of amino acids? A. Primary structure B. Secondary structure C. Enzyme D.Quaternary structure 3. What dictates the arrangement of the tertiary structure? A. Th…
See more on biologydictionary.net

Overview

Protein tertiary structure is the three dimensional shape of a protein. The tertiary structure will have a single polypeptide chain "backbone" with one or more protein secondary structures, the protein domains. Amino acid side chains may interact and bond in a number of ways. The interactions and bonds of side chains within a particular protein determine its tertiary structure. The protein tertiary structur…

Determinants

A protein folded into its native state or native conformation typically has a lower Gibbs free energy (a combination of enthalpy and entropy) than the unfolded conformation. A protein will tend towards low-energy conformations, which will determine the protein's fold in the cellular environment. Because many similar conformations will have similar energies, protein structures are dynamic, fluctuating between these similar structures.

History

The science of the tertiary structure of proteins has progressed from one of hypothesis to one of detailed definition. Although Emil Fischer had suggested proteins were made of polypeptide chains and amino acid side chains, it was Dorothy Maud Wrinch who incorporated geometry into the prediction of protein structures. Wrinch demonstrated this with the Cyclol model, the first prediction of the structure of a globular protein. Contemporary methods are able to determine, wi…

Determination

The knowledge of the tertiary structure of soluble globular proteins is more advanced than that of membrane proteins because the former are easier to study with available technology.
X-ray crystallography is the most common tool used to determine protein structure. It provides high resolution of the structure but it does not give information about protein's conformational flexibility.

Projects

The Folding@home project at Stanford University is a distributed computing research effort which uses approximately 5 petaFLOPS (≈10 x86 petaFLOPS) of available computing. It aims to find an algorithm which will consistently predict protein tertiary and quaternary structures given the protein's amino acid sequence and its cellular conditions.
A list of software for protein tertiary structure prediction can be found at List of protein structure …

See also

• Folding (chemistry)
• I-TASSER
• Nucleic acid tertiary structure
• Protein contact map
• Proteopedia

External links

• Protein Data Bank
• Display, analyse and superimpose protein 3D structures
• Alphabet of protein structures.
• Display, analyse and superimpose protein 3D structures

Tertiary Structure: The Overall 3-Dimensional Shape of A Protein

Image
A protein needs to adopt a final and stable 3-dimensional shape in order to function properly. The Tertiary Structureof a protein is the arrangement of the secondary structures into this final 3-dimensional shape. The sequence of amino acids in a protein (the primary structure) will determine where alpha helices and beta sheet…
See more on cbm.msoe.edu

Forces That Drive Tertiary Structure

  • Most proteins fold into their tertiary structure in an aqueous environment - a cell is, after all, 60% water. The chemical properties of the various R-groups (sidechains) of the amino acids within the protein chain will influence the way that the protein folds in its environment. When a protein is surrounded by water: 1. Hydrophobicamino acids will move away from the water and bury thems…
See more on cbm.msoe.edu

The Structure-Function Relationship

  • Proteins are amazing molecules because they come in a huge variety of sizes and shapes; each shape suited to perform a specific task. The primary sequence of amino acids in a protein determines its 3-dimensional shape which, in turn, determines how the protein will function. This structure-function relationship is key to appreciating proteins and protein structure. The same s…
See more on cbm.msoe.edu

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        total_videos
        33
        settings
        34
        url_current
        35
        menus
        36
        sidebar
        37
        i
        38
        __currentLoopData
        39
        loop
        40
        item
      • themes.DevBlog.panels.footer (resources/views/themes/DevBlog/panels/footer.blade.php)41blade
        Params
        0
        __env
        1
        app
        2
        errors
        3
        post
        4
        postContent
        5
        author
        6
        updated_at
        7
        bing_rich_snippet_text
        8
        bing_rich_snippet_link
        9
        bing_related_keywords
        10
        google_related_keywords
        11
        bing_news_title
        12
        bing_news_description
        13
        bing_videos
        14
        bing_images
        15
        bing_search_result_title
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        bing_search_result_description
        17
        bing_search_result_url
        18
        bing_paa_questions
        19
        bing_paa_answers
        20
        bing_slider_faq_questions
        21
        bing_slider_faq_answers
        22
        bing_pop_faq_questions
        23
        bing_pop_faq_answers
        24
        bing_tab_faq_questions
        25
        bing_tab_faq_answers
        26
        google_faq_questions
        27
        google_faq_answers
        28
        google_rich_snippet
        29
        google_search_result
        30
        indexedArray
        31
        total_images
        32
        total_videos
        33
        settings
        34
        url_current
        35
        menus
        36
        sidebar
        37
        i
        38
        __currentLoopData
        39
        loop
        40
        item
      • themes.DevBlog.panels.scripts (resources/views/themes/DevBlog/panels/scripts.blade.php)41blade
        Params
        0
        __env
        1
        app
        2
        errors
        3
        post
        4
        postContent
        5
        author
        6
        updated_at
        7
        bing_rich_snippet_text
        8
        bing_rich_snippet_link
        9
        bing_related_keywords
        10
        google_related_keywords
        11
        bing_news_title
        12
        bing_news_description
        13
        bing_videos
        14
        bing_images
        15
        bing_search_result_title
        16
        bing_search_result_description
        17
        bing_search_result_url
        18
        bing_paa_questions
        19
        bing_paa_answers
        20
        bing_slider_faq_questions
        21
        bing_slider_faq_answers
        22
        bing_pop_faq_questions
        23
        bing_pop_faq_answers
        24
        bing_tab_faq_questions
        25
        bing_tab_faq_answers
        26
        google_faq_questions
        27
        google_faq_answers
        28
        google_rich_snippet
        29
        google_search_result
        30
        indexedArray
        31
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        total_videos
        33
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        38
        __currentLoopData
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      uri
      GET {post}
      middleware
      web, checkdate
      as
      post.show
      controller
      App\Http\Controllers\Frontend\json_data\PostController@show
      namespace
      where
      file
      app/Http/Controllers/Frontend/json_data/PostController.php:18-166
      7 statements were executed5.07s
      receivinghelpdeskask
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        2.17ms/app/Providers/RouteServiceProvider.php:54receivinghelpdeskask
        Metadata
        Bindings
        • 0. 2025-05-10 06:45:21
        • 1. tertiary-structure-of-protein-example
        Backtrace
        • 15. /app/Providers/RouteServiceProvider.php:54
        • 18. /vendor/laravel/framework/src/Illuminate/Routing/Router.php:842
        • 19. Route binding:39
        • 20. /vendor/laravel/framework/src/Illuminate/Pipeline/Pipeline.php:167
        • 21. /vendor/laravel/framework/src/Illuminate/Foundation/Http/Middleware/VerifyCsrfToken.php:78
      • select * from `json_post_contents` where `json_post_contents`.`post_id` = 48644 and `json_post_contents`.`post_id` is not null and `rewrite_id` = 0
        46.42msmiddleware::checkdate:30receivinghelpdeskask
        Metadata
        Bindings
        • 0. 48644
        • 1. 0
        Backtrace
        • 19. middleware::checkdate:30
        • 20. /vendor/laravel/framework/src/Illuminate/Pipeline/Pipeline.php:167
        • 21. /vendor/laravel/jetstream/src/Http/Middleware/ShareInertiaData.php:61
        • 22. /vendor/laravel/framework/src/Illuminate/Pipeline/Pipeline.php:167
        • 23. /vendor/laravel/framework/src/Illuminate/Routing/Middleware/SubstituteBindings.php:50
      • select * from `nova_menu_menus` where `slug` = 'header' limit 1
        1.59ms/vendor/outl1ne/nova-menu-builder/src/helpers.php:32receivinghelpdeskask
        Metadata
        Bindings
        • 0. header
        Backtrace
        • 15. /vendor/outl1ne/nova-menu-builder/src/helpers.php:32
        • 17. /vendor/laravel/framework/src/Illuminate/Routing/Controller.php:54
        • 18. /vendor/laravel/framework/src/Illuminate/Routing/ControllerDispatcher.php:45
        • 19. /vendor/laravel/framework/src/Illuminate/Routing/Route.php:261
        • 20. /vendor/laravel/framework/src/Illuminate/Routing/Route.php:205
      • select * from `nova_menu_menu_items` where `nova_menu_menu_items`.`menu_id` = 1 and `nova_menu_menu_items`.`menu_id` is not null and `parent_id` is null order by `parent_id` asc, `order` asc, `name` asc
        2.51ms/vendor/outl1ne/nova-menu-builder/src/Models/Menu.php:35receivinghelpdeskask
        Metadata
        Bindings
        • 0. 1
        Backtrace
        • 19. /vendor/outl1ne/nova-menu-builder/src/Models/Menu.php:35
        • 20. /vendor/outl1ne/nova-menu-builder/src/helpers.php:33
        • 22. /vendor/laravel/framework/src/Illuminate/Routing/Controller.php:54
        • 23. /vendor/laravel/framework/src/Illuminate/Routing/ControllerDispatcher.php:45
        • 24. /vendor/laravel/framework/src/Illuminate/Routing/Route.php:261
      • select * from `nova_menu_menu_items` where `nova_menu_menu_items`.`parent_id` in (1) order by `order` asc
        780μs/vendor/outl1ne/nova-menu-builder/src/Models/Menu.php:35receivinghelpdeskask
        Metadata
        Backtrace
        • 24. /vendor/outl1ne/nova-menu-builder/src/Models/Menu.php:35
        • 25. /vendor/outl1ne/nova-menu-builder/src/helpers.php:33
        • 27. /vendor/laravel/framework/src/Illuminate/Routing/Controller.php:54
        • 28. /vendor/laravel/framework/src/Illuminate/Routing/ControllerDispatcher.php:45
        • 29. /vendor/laravel/framework/src/Illuminate/Routing/Route.php:261
      • select `id`, `post_title`, `slug` from `posts` where `status` = 'publish' and `posts`.`deleted_at` is null order by RAND() limit 10
        4.99s/app/View/Composers/SidebarView.php:22receivinghelpdeskask
        Metadata
        Bindings
        • 0. publish
        Backtrace
        • 14. /app/View/Composers/SidebarView.php:22
        • 15. /app/View/Composers/SidebarView.php:12
        • 16. /vendor/laravel/framework/src/Illuminate/View/Concerns/ManagesEvents.php:124
        • 17. /vendor/laravel/framework/src/Illuminate/View/Concerns/ManagesEvents.php:162
        • 20. /vendor/laravel/framework/src/Illuminate/View/Concerns/ManagesEvents.php:177
      • select * from `fake_users` where `fake_users`.`id` = 3406 limit 1
        31.24msview::2dd102cf0462e89a4d4d8bc77355d767652bf9aa:15receivinghelpdeskask
        Metadata
        Bindings
        • 0. 3406
        Backtrace
        • 21. view::2dd102cf0462e89a4d4d8bc77355d767652bf9aa:15
        • 23. /vendor/laravel/framework/src/Illuminate/Filesystem/Filesystem.php:108
        • 24. /vendor/laravel/framework/src/Illuminate/View/Engines/PhpEngine.php:58
        • 25. /vendor/livewire/livewire/src/ComponentConcerns/RendersLivewireComponents.php:69
        • 26. /vendor/laravel/framework/src/Illuminate/View/Engines/CompilerEngine.php:61
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      Outl1ne\MenuBuilder\Models\MenuItem
      1
      Outl1ne\MenuBuilder\Models\Menu
      1
      App\Models\JsonPostContent
      1
      App\Models\Post
      11
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          PHPDEBUGBAR_STACK_DATA
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          path_info
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          status_code
          200
          status_text
          OK
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          html
          content_type
          text/html; charset=UTF-8
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          request_server
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          array:55 [▼
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  ]
  "_flash" => array:2 [▶
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]