MODULE 5: Hemoglobin and Myoglobin, Lectures 12
Quadrant-2
Animations:
Myoglobin & Hemoglobin - Wiley
higheredbcs.wiley.com/legacy/college/boyer/0471661791/.../hbmb.htm
Because myoglobin and hemoglobin each bind oxygen, we can assume that there ... This
animation will cut cross-sectional slices through myoglobin, allowing ...
Myoglobin and Hemoglobin Structure Tutorial - Wiley
www.wiley.com/college/boyer/0470003790/structure/.../mbhb_intro.htm
Myoglobin & Hemoglobin ... The protein hemoglobin serves as the oxygen carrier in the
blood. It serves to increase the ... Oxidative Phosphorylation animation ...
Hemoglobin/Myoglobin Binding - YouTube ► 9:05► 9:05
www.youtube.com/watch?v=jhZCOtrqKdQ
Feb 6, 2011 - Uploaded by doorknobquestion. A short video clarifying myoglobin and
hemoglobin binding. This video reviews the curves associated with ...
Oxygen Binding by Myoglobin & Hemoglobin
www.bio.cmu.edu/courses/03231/LecF04/Lec13/lec13.html
Sep 21, 2004 - Lecture 13: O2 Binding by Myoglobin & Hemoglobin. smPDF Lecture
13 ... Hemoglobin Gallery of still pictures and animations. -by Dr. John ...
Myoglobin and Hemoglobin Structure - Tufts University
ase.tufts.edu/biology/MolecVisual/bio13/rightB13hemo.html
Hemoglobin subunit folding is similar to myoglobin. The Hemoglobin ... Myoglobin and
hemoglobin are proteins designed to carry oxygen. ... Replay animation
Lecture - 12 Myoglobin and Hemoglobin - Free Medical Video Lecture
www.learnerstv.com/video/Free-video-Lecture-1399-medical.htm
Free Lecture - 12 Myoglobin and Hemoglobin video lecture. ... Video Lectures, Video
Courses, Science Animations, Lecture Notes, Online Test, Lecture ...
Myoglobin & Hemoglobin | The World Of Biochemistry
theworldofbiochemistry.wordpress.com/videos/.../myoglobin-hemoglobi...
Myoglobin & Hemoglobin ... Animations · Other Videos · Podcasts · Mnemonics ·
General · Carbohydrate · Protein · Lipid · Enzymes · Hemoglobin · Hormones ...
PPT – Myoglobin and Hemoglobin PowerPoint ... - PowerShow.com
www.powershow.com/.../Myoglobin_and_Hemoglo...
Myoglobin and Hemoglobin - PowerPoint PPT Presentation ..... chart and diagram s for
PowerPoint with ...
Hemoglobin and Myoglobin - The Medical Biochemistry Page
themedicalbiochemistrypage.org/hemoglobin-myoglobin.php
The myoglobin and hemoglobin page provides a description of the structure and
function of these two oxygen-binding proteins.
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Proteins Lecture 11 Myoglobin and Hemoglobin spring 2012 animated
www.coursehero.com › Illinois
Proteins Lecture 11 Myoglobin (Mb) and Hemoglobin (Hb) Suggested Reading:
Lehninger, 5th edition, Chapter 5.1 Suggested Problems: Chapter 5 #1, 4 Why is ...
Haemoglobin - a molecular lung: 2
www3.ul.ie/~childsp/CinA/Issue65/TOC28_Haemoglobin.htm
Likewise, when oxyhaemoglobin (HbO2) loses dioxygen to myoglobin in a region .....
An animation of haemoglobin adding and losing dioxygen can be found at ...
Annotated Web Links Chapter 7 - Worth Publishers
www.worthpublishers.com/catalog/static/worth/.../bwl/lr07bw01.htm
Myoglobin and Hemoglobin ... has applet animations of the structural changes that
occur in hemoglobin as it ... SuperSecondary Structure: Myoglobin Module
Lecture on Myoglobin and Hemoglobin - BioSolutions
bio-solutions.blogspot.com › ... › myoglobin lecture
Lecture on Myoglobin and Hemoglobin. Myoglobin is a single-chain globular protein of
153 amino acids, containing a heme .... Anthrax Toxin Animation.
Hemoglobin - Proteopedia, life in 3D
www.proteopedia.org/wiki/index.php/Hemoglobin
Jan 28, 2014 - Human Hemoglobin α chain (grey and pink) β chain (green and yellow)
with bound O2 ... They are different but homologous, with a "globin fold" structure
similar to myoglobin. ... These movements are animated at this page.
Myoglobin Structure - 1CRO.com
www.1cro.com/campbell/.../myoglobintutorial/myoglobin.html
Myoglobin. Press the buttons as you read along to get an interactive illustration of
discussed concepts. Myoglobin and hemoglobin are proteins that serve all of ...
Illustrations:
Hemoglobin - Columbus Labs
www.columbuslabs.org/wp-content/uploads/2008/03/lecture16.pdf
Myoglobin is monomeric; hemoglobin is tetrameric ... 2. O. 2. -binding curves for
hemoglobin and myoglobin. ... chain. (Illustration: Irving Geis Rights owned.
Myoglobin & Hemoglobin - Wiley
www.wiley.com/college/boyer/0470003790/structure/.../EvalText.html
Because myoglobin and hemoglobin each bind oxygen, we can assume that ... is called
an allosteric (through space) interaction and is clearly illustrated in the
Oxygen Transport by Hemoglobin and Myoglobin - Wolfram ...►►
demonstrations.wolfram.com/OxygenTransportByH...
Hemoglobin, the essential component of red blood cells (erythrocytes), transports
oxygen ( ) through the ...
Page 2 of 14
Globular Hemeproteins | Lippincott's Illustrated Reviews: Biochemistry
https://www.inkling.com/read/illustrated...5th/.../globular-hemeproteins
In myoglobin and hemoglobin, one of these positions is coordinated to the side chain of
a histidine residue of the globin molecule, whereas the other position is ...
Biochemical Myoglobin and Haemoglobin/Hemoglobin Structure ...
nalinimarquez.hubpages.com › Education and Science
Here are some notes on myoglobin and hemoglobin that can be used for an
understanding or refresher that is helpful and useful for the ...
Oxygen Binding by Myoglobin & Hemoglobin
www.bio.cmu.edu/courses/03231/LecF04/Lec13/lec13.html
Sep 21, 2004 - Lecture 13: O2 Binding by Myoglobin & Hemoglobin. smPDF Lecture
... Myoglobin & Hemoglobin: Side-by-side Chime Images. -by Dr. Gordon ...
The Chemistry of Hemoglobin and Myoglobin
chemed.chem.purdue.edu/genchem/topicreview/bp/.../blood3.html
The site at which oxygen binds to both hemoglobin and myoglobin is the heme ...
Drawings of the structures of proteins often convey the impression of a fixed, ...
Oxygen Binding by Heme Proteins - Mathews/van Holde/Ahern 3rd ...
www.pearsonhighered.com/mathews/ch07/c07mobhp.htm
Throughout the myoglobin-hemoglobin family, the iron is chelated by a ... to heme is
illustrated in Figure 7.5, which shows the oxygenated form of myoglobin.
An Overview of Hemoglobin and Myoglobin | Interactive Biology, by ...
www.interactive-biology.com/.../an-overview-of-hemoglobin-a...
by Leslie Samuel - in 1,725 Google+ circles. The heme portion of myoglobin and
hemoglobin is extremely important ... As a result, hemoglobin and myoglobin are great
examples of
Heme B, The Important Component Of Hemoglobin And Myoglobin ...
www.shutterstock.com/.../stock-vector-heme-b-the-important-component...
Heme B, the important component of hemoglobin and myoglobin. Structural formula.
Stock Vector Illustration: Image ID: 107512988. Release Information: N/A.
myo-hemo
www.chem.uci.edu/~pfarmer/127i/myo-hemo.html
Myoglobin and hemoglobin function by reversibly binding dioxygen at heme ... active
site residues, such as the distal and proximal histidines, are illustrated.
Myoglobin Stock Illustrations. 6 Myoglobin clip art images and ...
www.canstockphoto.com/illustration/myoglobin.html
6 Myoglobin illustrations and clipart. ... Protein myoglobin with heme showed in balls
Clip Art ... Hemoglobin protein (Hb), chemical structure Stock Illustrations.
Heme A, The Important Component Of Hemoglobin And Myoglobin ...
www.shutterstock.co.in/.../stock-vector-heme-a-the-important-componen...
Heme A, the important component of hemoglobin and myoglobin. Structural formula.
Stock Vector Illustration: Image ID: 107512985. Release Information: N/A.
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myoglobin drawings
www.chem.ox.ac.uk/vrchemistry/chapter22/page24.htm
Globular Proteins: Myoglobin and Hemoglobin. The way in which the protein chain is
folded in the myoglobin molecule is shown (right). Myoglobin has 153 ...
Carbon Monoxide Binding by Hemoglobin and Myoglobin under ...
www.pnas.org/content/69/4/868.full.pdf
by M Brunori - 1972 - Cited by 37 - Related articles
light intensity for both myoglobin and hemoglobin, as shown by Fig. 2. The effect of ....
case illustrated in the accompanying Scheme 1, where the small arrows ...
Simultaneous Determination of Hemoglobin and Myoglobin Oxygen ...
www.researchgate.net/.../249330727_Simultaneous_Determination_of_He...
ABSTRACT A completely optical method is described for the simultaneous
determination of hemoglobin and myoglobin oxygen saturation. Solution oxygen ...
2</sub>-Binding Curve for Hemoglobin and Myoglobin
www.elsevierimages.com/image/34116.htm
Rights-managed labeled illustration of O 2 -Binding Curve for Hemoglobin and
Myoglobin.
Comparative analysis of autoxidation of haemoglobin
jeb.biologists.org/content/204/11/2029.full.pdf
by FB Jensen - 2001 - Cited by 20 - Related articles
The rate of autoxidation of haemoglobin and myoglobin is several orders of ....
Examples of individual experiments (chosen as those at which the individual k ...
Myoglobin - Encyclopedia of Life Sciences
www.els.net/WileyCDA/ElsArticle/refId-a0000656.html
Myoglobin is an oxygen‐binding haem protein of vertebrate and invertebrate ... The
axial histidine, proximal histidine (His93) and haem are illustrated in the stick model. ...
of proximal histidine proton NMR peaks in myoglobin and hemoglobin.
Myoglobin - Merriam-Webster Online
www.merriam-webster.com/dictionary/myoglobin
Definition of myoglobin from the Merriam-Webster Online Dictionary with audio
pronunciations, thesaurus, Word of the Day, and word games. ... a red iron-containing
protein pigment in muscles that is similar to hemoglobin ... illustrations.
Oxygen Binding Proteins II: Hemoglobin - Michael P. Ready
michaelpready.com/mready/Oxygen%20Binding%20Proteins%20II.htm
Myoglobin is admirably suited for storing oxygen and delivering it to the muscle ... The
illustration below shows how the sigmoidal binding curve can be thought ...
Heme B, the important component of hemoglobin and myoglobin ...
depositphotos.com/.../stock-illustration-Heme-B-the-important-compone...
Oct 3, 2012 - ... of premium high-resolution stock photos, vector images and
illustrations. ... component of hemoglobin and myoglobin - Stock Illustration.
Chapter 7 Hemoglobin: Portrait of a Protein in Action
ocw.sogang.ac.kr/rfile/.../biochemistry7e_ch07_20130620145200.pdf
7.1 Myoglobin and Hemoglobin Bind Oxygen at Iron Atoms in Heme ... With the use of
appropriate techniques, images can be generated that reveal differences ...
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Video demonstrations:
Myoglobin and Hemoglobin Video Lecture, IIT Kharagpur
freevideolectures.com › ... › IIT Kharagpur
Myoglobin and Hemoglobin Video Lecture, IIT Kharagpur Course, Bio Technology,
Youtube Free Download ...
Getting Oxygen: Myoglobin vs. Hemoglobin - YouTube ► 6:19► 6:19
www.youtube.com/watch?v=91c04OoTEJs
Uploaded by ThePenguinProf. Hemoglobin. ... You need Adobe Flash Player to watch
this video. .... Hemoglobin/Myoglobin Bindingby ...
Hemoglobin/Myoglobin Binding - YouTube ► 9:05► 9:05
www.youtube.com/watch?v=jhZCOtrqKdQ
Feb 6, 2011 - Uploaded by doorknobquestion
A short video clarifying myoglobin and hemoglobin binding. This video reviews the
curves associated with ...
Video - Lecture - 12 Myoglobin and Hemoglobin - Foldit Wiki - a ...
foldit.wikia.com/wiki/File:Lecture_-_12_Myoglobin_and_Hemoglobin
Lecture - 12 Myoglobin and Hemoglobin. Edit. History ... Thought I would start a page
linking through to some Biochem videos for anyone that is... See full list > ...
Lecture - 12 Myoglobin and Hemoglobin - Free Medical Video Lecture
www.learnerstv.com/video/Free-video-Lecture-1399-medical.htm
Free Lecture - 12 Myoglobin and Hemoglobin video lecture.
Myoglobin & Hemoglobin | The World Of Biochemistry
theworldofbiochemistry.wordpress.com/videos/.../myoglobin-hemoglobi...
Myoglobin & Hemoglobin ... Animations · Other Videos · Podcasts · Mnemonics ·
General · Carbohydrate · Protein · Lipid · Enzymes · Hemoglobin · Hormones ...
Lecture 12: Myoglobin and Hemoglobin | CosmoLearning Biology
www.cosmolearning.com/video-lectures/myoglobin-and-hemoglobin/
Apr 12, 2009 - This video lecture, part of the series Biochemistry I by Prof. S.
Dasgupta, does not currently have a detailed description and video lecture title.
Lecture - 12 Myoglobin and Hemoglobin ,molecular biology ...
www.onlinevideolecture.com/medical-science/.../index.php?course...
Lecture - 12 Myoglobin and Hemoglobin ,molecular biology ,nptelhrd course video
tutorials and Lectures.
Oxygen Binding by Myoglobin and Hemoglobin - SlideShare
www.slideshare.net/alecksmadrona/oxygen-binding-by
Jul 28, 2013 - Madrona, Vivien Alexandra C. 3Bio5 College of Science University of
Santo Tomas Espana, Manila Oxygen binding by Myoglobin ...
Myoglobin and Hemoglobin -Video lecture Series -Watch Online for ...
bimatics.blogspot.com/.../myoglobin-and-hemoglobin-video-lecture.htm...
... -Watch Online for free. Tuesday, December 16, 2008 Suresh kumar No comments.
Myoglobin and Hemoglobin -Video lecture Series -Watch Online for free ...
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Myoglobin Videos - Metacafe
www.metacafe.com/videos_about/myoglobin/
In honor of the release of Riddick, a movie absolutely no one was asking for, we
decided to point ... A short video clarifying myoglobin and hemoglobin binding.
PPT – Protein Function MyoglobinHemoglobin PowerPoint ...
www.powershow.com/.../Protein_Function_Myoglo...
Protein Function MyoglobinHemoglobin - PowerPoint PPT Presentation ..... to receive
the free Protein Bar in ...
Quadrant-3
Multiple choice questions – chose the correct answer:
1. The dissociation constant is
a) a measure of how easily the alpha and beta subunits combine to form hemoglobin.
b) the inverse of the Hill coefficient.
c) the inverse of the association constant.
d) related to the enthalphy change due to ligand binding.
2. Allosteric effects that occur in hemoglobin
a) are important for maintaining Fe in the Fe2+ state.
b) minimize oxygen delivery to the tissues.
c) optimize oxygen delivery to the tissues.
d) can also be observed in myglobin.
3. The cooperativity of O 2 binding to hemoglobin results in a
a) 100-fold higher affinity for the last O 2 bound than for the first.
b) 100-fold lower affinity for the last O 2 bound than for the first.
c) extensive protein conformational change.
d) The first and third choices are both correct.
4. In deoxy hemoglobin (Hb), the Fe (II) is 5-coordinated to
a) four nitrogens of heme and to the proximal His of Hb.
b) four nitrogens of heme and to a water molecule.
c) four nitrogens of heme and to an O 2 molecule.
d) two nitrogens of heme and to three His residues in Hb.
5. Each myoglobin molecule is capable of binding one oxygen, because
a) Theprotein molecule is tightly bound
b) Myoglobin contains one heme per molecule
c) Hemoglobin is small to accommodate
d) All the above
6. Spontaneous oxidation of the heme-bound Fe(II) to Fe(III) is prevented in hemoglobin by
a) the symmetry of its quaternary structure.
b) the four heme-protein covalent bonds.
c) a highly-ordered water molecule within the heme pocket.
d) methemoglobin reductase.
Page 6 of 14
7. In sickle cell anemia, the basis of the malfunction of the hemoglobin molecule is:
a) incorrect secondary structure.
b) substitution of a single amino acid.
c) faulty binding of the heme groups.
d) reduced affinity for oxygen.
8. The red colour of haemoglobin is due to
a) Protein conformation
b) Multiple subunits of proteins
c) Presence of heme group
d) None of the above
9. The following statements are about hemoglobin and myoglobin. Please select the most
correct one:
a) Hemoglobin has 4 subunits while myoglobin has one subunit.
b) Hemoglobin binds 4 molecules of oxygen while myoglobin binds one molecule of
oxygen.
c) Hemoglobin transports oxygen to all cells while myoglobin releases oxygen in muscle
cells when needed.
d) All of above.
10. The transportation of oxygen by hemoglobin is important because
a) O 2 diffusion alone is too poor for transport in larger animals.
b) Solubility of O 2 is low in plasma i.e. 10-4 M.
c) But bound to hemoglobin, [O 2 ] = 0.01 M or that of air
d) All the above are important
11. Myoglobin facilitates rapidly respiring muscle tissue because
a) The rate of O 2 diffusion from capillaries to tissue is slow because of the solubility of
oxygen.
b) Myoglobin increases the solubility of oxygen.
c) Myoglobin facilitates oxygen diffusion.
d) All of the above are correct
12. The Bohor effect sates that
a) Higher pH promotes tighter binding of oxygen to hemoglobin
b) Lower pH permits the easier release of oxygen from hemoglobin
c) A shift in the equilibrium will influence the amount of oxygen binding
d) All of the above are correct
State whether True or False:
1. In sickle cell anemia, the basis of the malfunction of the hemoglobin molecule is
insufficient iron in the diet.
2. Hemoglobin is a tetramer composed of two different types of globin subunits, each of
which has an O 2 binding site
3. The oxygen dissociation curve for myoglobin has a hyperbolic shape
4. Allosteric effects that occur in haemoglobin is to optimize oxygen delivery to the
tissues
Page 7 of 14
5. The binding of one O 2 to a molecule of hemoglobin results in an increased affinity for
O 2 in the remaining subunits
6. Both hemoglobin and myoglobin are tetrameric proteins.
7. Fetal hemoglobin is composed of two α and two γ subunits.
8. The binding of each O 2 molecule to hemoglobin decreases its affinity for the next O 2 .
9. In hemoglobin, the iron of the heme is bonded to the four nitrogens of porphyrin and
to the proximal histidine residue of the globin chain.
10. Heme of both hemoglobin and myoglobin is a prosthetic group.
Fill in the blanks:
1. The Hill coefficient (nH) for myoglobin is ____; whereas nH is about ___ for
hemoglobin.
2. The cooperativity of O 2 binding to hemoglobin results in a ____________-fold higher
affinity for the last O 2 bound than for the first.
3. The slope of a Hill plot for hemoglobin ______; whereas that for myoglobin _______.
4. Similarities between hemoglobin and myoglobin include ____________________
5. Hemoglobin exists in two alternate conformations __________ state and
______________
6. __________________is contained in the heme portion of hemoglobin and myoglobin.
7. ____________ This is a genetic disease due to the decreased production of one of the
subunits of haemoglobin
8. ____________ type of hemoglobin is composed of two α chains and two γ chains
9. ____________ is the molecule whose function is to store oxygen is muscle cells
10. ____________ type of binding is indicated by a sigmoidal-shaped binding curve.
11. In hemoglobin, the iron of the heme is bonded to the four nitrogens of porphyrin and
to the proximal ______________ residue of the globin chain
12. The effect of pH on oxygen-binding of hemoglobin is referred to as the
_____________.
Assignments (questions and solutions):
1. What are myoglobins and hemoglobins?
2. Discuss briefly on myoglobin polypeptide chain and heme cofactor
3. Explain briefly on the structure of a hemoglobin Subunit
4. Give details on different steps involved i the path of Oxygen Delivery in the Body
5. How do understanding the Hemoglobin and Myoglobin Dissociation Curves are
useful?
6. Discuss briefly on shifts in the Hemoglobin Dissociation Curve
7. What are the different roles of hemoglobin and myoglobin
Quadrant – 4
Page 8 of 14
Supplementary Reading:
1. Allyn and Bacon (1983) Organic Chemistry, Morrison and Boyd.
2. Stryer L (1975) Biochemistry, W.H. Freeman and Co, San Francisco.
3. Liang, Yuhe et al. 2001. The Crystal Structure of Bar-headed Goose Hemoglobin in
Deoxy Form: The Alloseteric Mechanism of a Hemoglobin Species with High
Oxygen Affinity. Journal of Molecular Biology 313: 123-137.
4. Mathews, Christopher, Kensal Van Holde and Kevin Ahern (2005) Biochemistry 3 rd
edition. http://www.aw-bc.com/mathews/ch07/c07emhp.htm.
5. Natzke, Lisa (2005) Hemoglobin.
http://biology.kenyon.edu/BMB/Chime/Lisa/FRAMES/hemetext.htm.
Wiki development on the course/other resources:
Myoglobin - Wikipedia, the free encyclopedia
en.wikipedia.org/wiki/Myoglobin
Myoglobin is an iron- and oxygen-binding protein found in the muscle tissue of
vertebrates in general and in almost all mammals. It is related to hemoglobin, ...Meat
color - Role in disease - Structure and bonding - Synthetic analogues
Essential Biochemistry - Myoglobin and Hemoglobin - Wiley
www.wiley.com/college/pratt/.../myoglobin_hemoglobin/index.html
INTRODUCTION. Myoglobin and hemoglobin are globular proteins that serve to bind
and deliver oxygen. These globins dramatically improve the concentration ...
Hemoglobin and Myoglobin - CliffsNotes
www.cliffsnotes.com › Sciences › Biochemistry I
Hemoglobin and myoglobin are only slightly related in primary sequence. Although
most amino acids are different between the two sequences, the amino acid ...
Structural Biochemistry/Protein function/Heme group/Myoglobin ...
en.wikibooks.org/wiki/Structural_Biochemistry/Protein.../Myoglobin
Myoglobin is a protein found in muscles that binds oxygen with its heme group like
hemoglobin. Heme group consists of protoporphyrin organic component and ...
Hemoglobin and Myoglobin - The Medical Biochemistry Page
themedicalbiochemistrypage.org/hemoglobin-myoglobin.php
The myoglobin and hemoglobin page provides a description of the structure and
function of these two oxygen-binding proteins.
An Overview of Hemoglobin and Myoglobin | Interactive Biology, by ...
www.interactive-biology.com/.../an-overview-of-hemoglobin-a...by Leslie Samuel - in 1,729
Google+ circles. Jun 7, 2012 - Hemoglobin and myoglobin are two of the most
important proteins in the body. They are a great example of the old biology maxim,
structure ...
Page 9 of 14
Myoglobin and Hemoglobin - UF Macromolecular Structure Group
msg.mbi.ufl.edu/bch4024r/notes-L10.2009.pdf
Myoglobin and hemoglobin are hemeproteins whose physiological importance is
principally related to their ability to bind molecular oxygen. Myoglobin and ...
Oxygen Transport by Hemoglobin and Myoglobin - Wolfram ... ►►
demonstrations.wolfram.com/OxygenTransportByH...
Hemoglobin, the essential component of red blood cells (erythrocytes), transports
oxygen ( ) through the ...
Myoglobin and Hemoglobin Myoglobin structure Heme Oxygen ...
www.olemiss.edu/depts/chemistry/courses/chem471_99/L12_6.pdf
Lecture 12. 1. Myoglobin and Hemoglobin. • Myoglobin structure - a monomer. – Iron
complexed by Heme, surrounded by protein. • Hemoglobin structure - a ...
Heme, Myoglobin, Hemoglobin - It works!
biotka.mol.uj.edu.pl/zbm/handouts/.../Lecture-2_(heme)_Mb_Hb.pdf.pd...
relatively spherical in shape as the name implies. Common globular proteins include
egg albumin, hemoglobin, myoglobin, insulin, serum globulins in blood, ...
Hemoglobin Myoglobin Lecture.doc
utcom2011.wikispaces.com/.../Hemoglobin%20Myoglobin%20Lecture...
Hemoglobin Myoglobin Lecture. Objectives. 1) Describe the structure of the globin
fold. It is dominated by alpha helices and is connected to the heme group via ...
O 2 Binding by Myoglobin & Hemoglobin
www.bio.cmu.edu/courses/03231/MCQF04/MCQLec13.htm
Quiz on Lecture 13: O2 Binding by Myoglobin & Hemoglobin. 1. The dissociation
constant is. a measure of how easily the alpha and beta subunits combine to ...
Hemoglobin and Myoglobin
www.uh.edu/sibs/faculty/glegge/lecture_13.ppt
Protein Function. Globins and Antibodies. 3/10/2003. Hemoglobin and Myoglobin.
Because of its red color, the red blood pigment has been of interest since ...
Myoglobin, Hemoglobin and Allosteric Regulation
people.virginia.edu/~dta4n/biochem503/hb.html
This tutorial shows how myoglobin and hemoglobin bind oxygen. Aspects of the
changes in hemoglobin structure that accompany oxygen binding are also ...
Lecture - 12 Myoglobin and Hemoglobin - Foldit Wiki - Wikia
foldit.wikia.com/wiki/File:Lecture_-_12_Myoglobin_and_Hemoglobin
Lecture - 12 Myoglobin and Hemoglobin. Edit. History · Talk0. 805pages on this wiki.
From Youtube. 7 Views. About; File History; Metadata. There is no ...
Oxygen Binding by Myoglobin and Hemoglobin - SlideShare
www.slideshare.net/alecksmadrona/oxygen-binding-by
Jul 28, 2013 - Madrona, Vivien Alexandra C. 3Bio5 College of Science University of
Santo Tomas Espana, Manila Oxygen binding by Myoglobin ...
Page 10 of 14
Solution to Quiz:
Chose the correct answer
1. C 6. A 11 D
2. C 7. B 12 D
3. D 8. C
4. A 9. D
5. B 10. d
State whether True or False
1. F 3. F 5. T 7. T 9. T
2. T 4. T 6. F 8. F 10 T
t
Fill in the Blanks
1. 1 4. nH=3 7. Sickle cell 10 Cooperative
anaemia
2. 3 5. nH=1 8. Foetal Hb 11 His
3. Several/100 6. Oxygen binding, 9. Myoglobin 12 Bohr’s effect
heme
Answers are only indicative. Expand on the outline given:
1. What are myoglobins and hemoglobins?
Myoglobin and hemoglobin are proteins designed to carry oxygen. Hemoglobin carries
oxygen from the lungs to the tissues. Myglobin is the oxygen storage protein of the
muscle. The richest source of myoglobin is the muscle of aquatic diving mammals, such
as seals or whales, since these tissues need a very rich store of oxygen to see them
through long anoxic periods during a dive. It serves as an oxygen reservoir, picking up
O 2 from the hemoglobin and delivering it to the cells as O 2 is used up in metabolism.
Sperm whale myoglobin consists of 153 amino acids (Mw = 17,199).
Page 11 of 14
2. Discuss briefly on myoglobin polypeptide chain and heme cofactor
Myoglobin protein shows the backbone of the single peptide chain that makes up. The
peptide twists and turns to form a relatively compact globular structure. In addition to
the protein components, both myoglobin (Mb) and hemoglobin (Hb) require a non-
amino acid component to actually complex with the bound oxygen. Such non-amino acid
components are called "cofactors" or "coenzymes" or "prosthetic groups", more or less
interchangeably. The prosthetic group of both Hb and Mb is the heme group, also found
in cytochromes and in enzymes such as catalase. The heme group is made up of four
fused five member rings to form a planar structure with four nitrogens projecting toward
the center and various side groups projecting away from the ring. The nitrogen ring
structure is just the right size and shape to form a coordination complex with iron in its
+2 oxidation state (ferrous iron). Myoglobin and hemoglobin are unusual in that they
contain only alpha helix secondary structure linked together by stretches of random coil.
3. Explain briefly on the structure of a hemoglobin Subunit
Hemoglobin consists of 2 alpha subunits and 2 beta subunits to give a four chain
structure. Although the alpha subunit sequence is quite different from the sequence of
myoglobin, the hemoglobin structure also contains only the alpha helical segments in the
same number and relative orientation as in myoglobin. While there are a number of
interactions between the alpha and beta subunits, the two alpha subunits are far enough
apart that there are few interactions, while strong interactions occur between alpha and
beta subunits. The overall pattern of interchain patterns makes up the quaternary
structure. In deoxyhemoglobin the quaternary structure is such that a relatively large
central cavity is formed between the four subunits. When oxygen binds to the hemes,
there is a relatively small conformational change in the tertiary structure of each subunit
which results in a larger change in the interactions between the individual subunits (i.e
the quaternary structure), narrowing the central cavity. This is a crucial factor in the
ability of hemoglobin to bind oxygen in the lungs and to release it in the tissues.
4. Give details on different steps involved i the path of Oxygen Delivery in the Body
The delivery of oxygen to tissue in the human body follows the following path:
• Oxygen is inhaled into the lungs
• Oxygen diffuses into the alveoli of the lungs
• Oxygen binds to hemoglobin in the blood in the alveoli
• The oxygenated hemoglobin travels through the arteries until it gets to the
capillaries
• Hemoglobin releases oxygen in the capillaries according to the Hemoglobin
Page 12 of 14
5. How do understanding the Hemoglobin and Myoglobin Dissociation Curves are
useful?
The Hemoglobin and Myoglobin Dissociation Curves, when taken together, represent an
important relationship in the delivery of oxygen to exercising muscle. Myoglobin is a
molecule in the muscle that binds and releases oxygen according to the Myoglobin
Dissociation Curve. This acts as a reserve of oxygen and can help facilitate the transport
of oxygen. When oxygen diffuses through interstitial fluids, the amount of oxygen
dissolved in the fluid is called the Partial Pressure of Oxygen and is represented as PO 2 .
Oxygen diffuses from areas with high levels of PO 2 to areas with low levels of PO 2 .
The Hemoglobin and Myoglobin Dissociation Curves show the relationship between the
PO 2 in the fluids and the Oxygen Saturation of the oxygen binding molecules. Curves A
and B in the graph below represent Hemoglobin and Myoglobin, respectively.
The Myoglobin Dissociation Curve does not change significantly at normal physiologic
chemistries. The Hemoglobin Dissociation Curve does shift left and right under
physiologic conditions that normally occur during exercise.
6. Discuss briefly on shifts in the Hemoglobin Dissociation Curve
The following 4 factors all cause the Hemoglobin Dissociation Curve to shift to the
RIGHT.
• Decreasing pH (More Acidic)
• Increasing Temperature
• Increasing dissolved Carbon Dioxide
• Increasing DPG (diphosphoglycerate)
When the Hemoglobin Dissociation Curve shifts to the right, it allows the hemoglobin
to release its oxygen more easily. This is important because this means that a low SmO 2
(muscle oxygen saturation) value doesn’t always indicate that there is insufficient
oxygen available for the mitochondria. The converse of these factors causes the
Hemoglobin Dissociation Curve to shift to the left, which means that a high SmO 2 value
doesn’t always indicate there is plenty of oxygen available for the mitochondria.
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7. What are the different roles of hemoglobin and myoglobin
Hemoglobin and myoglobin are proteins that have evolved to carry out the specialized
functions of oxygen transport and storage in animals. Animals must ensure a steady
supply of oxygen to body cells and remove metabolic waste products such as carbon
dioxide. Diffusion transport through tissues is generally not fast enough. Almost all
animals except insects pump oxygen in the blood through arteries to the tissues and
return carbon dioxide via venous blood to lungs or gills. All higher organisms have
oxygen transport proteins, which allow the blood to carry a much greater load of oxygen
than would be permitted by solubility alone. Oxygen transport proteins may be either
dissolved in the blood (as in some invertebrates) or concentrated in specialized cells, like
the human erythrocytes. In all vertebrates the oxygen transport protein is hemoglobin, a
protein that can pick up oxygen in lungs or gills and deliver it to tissues. Myoglobin, by
contrast, is an oxygen storage protein. Oxygen transported to tissues must be released for
utilization. In tissues, such as muscle, with high oxygen demands, myoglobin provides
large oxygen reserves.
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