To explain:
The classification of bones by shapes.
Introduction:
Bone is the hardest structure present in the body. It is whitish color. The bones require calcium ion which makes it stronger. The bone makes the skeletal structure of the body and mainly consists of calcium phosphate and calcium carbonate. It plays an important role in calcium storage and releases calcium to the blood.
![Check Mark](/static/check-mark.png)
Explanation of Solution
There are four different types of bones present in the body that are classified according to their shapes. The four types of bones are:long bones, short bones, flat bones, and irregular bones.
The detail description of .different types of bones are listed below:
(1)
Long bones:
The long bones are comprised of longitudinal axes along with the expanded ends. For example:forearm bones and thigh bones.
(2)
Short bones:
The short bones have a cubical structures and its length and widths are roughly equal. The examples of short bones are the bones present in wrists and ankles. The sesamoid bone is a short bone having a round shape. The bone present in the tendon area and the patella (kneecap) bone is also a sesamoid type of bone.
(3)
Flat bones:
The flat bones are comprised of plate-like structure having broad surfaces. The flat bones are present in the ribs, scapulae, and skull bones. Some of the skull bones are flat bones.
(4)
Irregular bones:
The irregular bones consist of different shapes and are connected to other bones. The irregular bones are present in the backbone of vertebrate and the facial bones.
There are four different types of bones present in the body. They are long bones, short bones, flat bones, and irregular bones.
Want to see more full solutions like this?
Chapter 7 Solutions
HOLES HUMAN ANATOMY AND PHYSIOLOGY
- What type of structure(s) would you expect to see in peripheral membrane proteins? (mark all that apply) A. Amphipathic alpha helix (one side is hydrophilic and one side is hydrophobic) B. A hydrophobic beta barrel C. A hydrophobic alpha helix D. A chemical group attached to the protein that can anchor it to the membranearrow_forwardTemporal flexibility (the ability to change over time) of actin structures within a cell is maintained by… A. The growth/shrinkage cycle B. Periodic catastrophe C. GTP hydrolysis D. Treadmilling E. None of the abovearrow_forwardDuring in vitro polymerization of actin and microtubule filaments from their subunits, what causes the initial delay in filament growth? A.Nucleation B.Reaching homeostasis C.Nucleotide exchange D.ATP or GTP hydrolysis E.Treadmillingarrow_forward
- You expect to find which of the following in the Microtubule Organizing Center (MTOC)...(mark all that apply) A. Gamma tubulin B. XMAP215 C. Centrioles D. Kinesin-13arrow_forwardThe actin-nucleating protein formin has flexible “arms” containing binding sites that help recruit subunits in order to enhance microfilament polymerization. What protein binds these sites? A.Thymosin B.Profilin C.Cofilin D.Actin E.Tropomodulinarrow_forwardWhile investigating an unidentified motor protein, you discover that it has two heads that bind to actin. Based on this information, you could confidently determine that it is NOT... (mark all that apply) A. A myosin I motor B. A dynein motor C. A myosin VI motor D. A kinesin motorarrow_forward
- You isolate the plasma membrane of cells and find that . . . A. it contains regions with different lipid compositions B. it has different lipid types on the outer and cytosolic leaflets of the membrane C. neither are possible D. A and B both occurarrow_forwardYou are studying the mobility of a transmembrane protein that contains extracellular domains, one transmembrane domain, and a large cytosolic domain. Under normal conditions, this protein is confined to a particular region of the membrane due to the cortical actin cytoskeletal network. Which of the following changes is most likely to increase mobility of this protein beyond the normal restricted region of the membrane? A. Increased temperature B. Protease cleavage of the extracellular domain of the protein C. Binding to a free-floating extracellular ligand, such as a hormone D. Protease cleavage of the cytosolic domain of the protein E. Aggregation of the protein with other transmembrane proteinsarrow_forwardTopic: Benthic invertebrates as an indicator species for climate change, mapping changes in ecosystems (Historical Analysis & GIS) What objects or events has the team chosen to analyze? How does your team wish to delineate the domain or scale in which these objects or events operate? How does that limited domain facilitate a more feasible research project? What is your understanding of their relationships to other objects and events? Are you excluding other things from consideration which may influence the phenomena you seek to understand? Examples of such exclusions might include certain air-born pollutants; a general class of water bodies near Ottawa, or measurements recorded at other months of the year; interview participants from other organizations that are involved in the development of your central topic or issue. In what ways do your research questions follow as the most appropriate and/or most practical questions (given the circumstances) to pursue to better understand…arrow_forward
- The Esp gene encodes a protein that alters the structure of the insulin receptor on osteoblasts and interferes with the binding of insulin to the receptor. A researcher created a group of osteoblasts with an Esp mutation that prevented the production of a functional Esp product (mutant). The researcher then exposed the mutant strain and a normal strain that expresses Esp to glucose and compared the levels of insulin in the blood near the osteoblasts (Figure 2). Which of the following claims is most consistent with the data shown in Figure 2 ? A Esp expression is necessary to prevent the overproduction of insulin. B Esp protein does not regulate blood-sarrow_forwardPredict the per capita rate of change (r) for a population of ruil trees in the presence of the novel symbiont when the soil moisture is 29%. The formula I am given is y= -0.00012x^2 + 0.0088x -0.1372. Do I use this formula and plug in 29 for each x variable?arrow_forwardPlease answer the following chart so I can understand how to do it.arrow_forward
- Human Anatomy & Physiology (11th Edition)BiologyISBN:9780134580999Author:Elaine N. Marieb, Katja N. HoehnPublisher:PEARSONBiology 2eBiologyISBN:9781947172517Author:Matthew Douglas, Jung Choi, Mary Ann ClarkPublisher:OpenStaxAnatomy & PhysiologyBiologyISBN:9781259398629Author:McKinley, Michael P., O'loughlin, Valerie Dean, Bidle, Theresa StouterPublisher:Mcgraw Hill Education,
- Molecular Biology of the Cell (Sixth Edition)BiologyISBN:9780815344322Author:Bruce Alberts, Alexander D. Johnson, Julian Lewis, David Morgan, Martin Raff, Keith Roberts, Peter WalterPublisher:W. W. Norton & CompanyLaboratory Manual For Human Anatomy & PhysiologyBiologyISBN:9781260159363Author:Martin, Terry R., Prentice-craver, CynthiaPublisher:McGraw-Hill Publishing Co.Inquiry Into Life (16th Edition)BiologyISBN:9781260231700Author:Sylvia S. Mader, Michael WindelspechtPublisher:McGraw Hill Education
![Text book image](https://www.bartleby.com/isbn_cover_images/9780134580999/9780134580999_smallCoverImage.gif)
![Text book image](https://www.bartleby.com/isbn_cover_images/9781947172517/9781947172517_coverImage_Textbooks.gif)
![Text book image](https://www.bartleby.com/isbn_cover_images/9781259398629/9781259398629_smallCoverImage.gif)
![Text book image](https://www.bartleby.com/isbn_cover_images/9780815344322/9780815344322_smallCoverImage.gif)
![Text book image](https://www.bartleby.com/isbn_cover_images/9781260159363/9781260159363_smallCoverImage.gif)
![Text book image](https://www.bartleby.com/isbn_cover_images/9781260231700/9781260231700_smallCoverImage.gif)