Question 8- A-) Protein structure- Describe how the following two inte.docx
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Question 8. A.) Protein structure. Describe how the following two interactions are critical in protein structure: (i) hydrogen bonds between backbone atoms in the formation of secondary structure elements, and (ii) hydrophobic side chains in the formation of the hydrophobic core of a protein. In your answer explain the chemical structure of the protein backbone, describe hydrogen bonding in alpha-helices and beta-sheets, and explain the difference between hydrophilic and hydrophobic amino acids. B.) Protein families . Describe (i) how the process of molecular evolution generates protein families, and (ii) how the amino acid sequence alignments based on sequence similarities for such members of a protein family can be used to identify conserved regions of a protein and construct a phylogenetic tree of such members of a protein family. (iii) Will amino acids at the active site of an enzyme tend to be conserved in a protein family? Why? C.) Protein evolution. (i) Illustrate the phenomenon of functional sequence variation using antibodies that can bind to a range of different antigens. (ii) Explain the process of domain shuffling in protein evolution and give an example of how this process can generate proteins with novel functions. .
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Proteins fold. How WhySolutionANSProtein folding Protein.pdf
Proteins fold. How? Why?
Solution
ANS:
Protein folding: Proteins are the molecules in the body which carries out many important
functions, such as enzymes and antibodies.
Before proteins carry out their function, they must first assemble themselves or fold.
PROTEIN FOLDING MODELS:
1. Frame work model:
In this the protein local elements which are stretches of amino acids liked by one another by
covalently with peptide bonds. The region of the primary amino acids sequence in peptide bonds
make different domains.in this domains some of regions are made with Alfa - helix and some are
beta sheet domains.
These primary elements form secondary structure independently of tertiary structure (kim and
baldwin).these elements can diffuse until they collided, successfully adhering and coalescing to
give the tertiary structure (diffus-collision model), (karplus and weaven).
2. The classic nucleation model:
It postulates that some neighboring residues in the sequence would form native secondary
structure that would act as a nucleus form which the native structure would propagate in a step
wise manner. Thus the tertiary structure would form as necessary consequence of the secondary
structure (wetlaufer).
3. Hydrophobic collapse model:
It is hypothesized that a protein would collapse rapidly around its hydrophobic side chain and
then arrange from restricted conformational space occupied by the intermediate. Here the
secondary structure would be directed by native like tertiary structure (ptitsyn & kwajima).
Leviathal’s paradox:
It is formulated by Cyrus Leviathal. It explains, there are vast too many different possible
conformations for a protein to fold by a random search.
Structural organization of protein:
1. Primary Structure: the sequence of amino acids along with the di sulphide bonds.
2. SECONDARY STRUCTURE:
Alfa Helices and Beta- Pleated sheets are most frequently occur in secondary structure in
polypeptides. Both of these can case local folding of protein.
The Alfa Helices in polypeptide made up of L- Alfa amino acids are right handed, the Alfa -
Helices is stabilized by hydrogen bonds formed between oxygen and amide hydrogen’s of
peptide bonds that are a part of linear sequence.
Beta- Pleated sheets: 2 types
A. Parallel: in this the adjacent hydrogen bonding segments are connected by cross over
connection [Right handed].
B. Anti-Parallel: In this the adjacent hydrogen bonding segments are connected by HAIRPIN
turns or reverse turn [Left Handed].
3. Tertiary structure: It is arisen because of the folding of poly peptides upon itself.
4. Quaternary structure:
Some proteins are made up of 2 or more polypeptides chains, the interaction between different
poly peptide are subunits gives rise to the quaternary structure..
What are the advantages for proteins to form three-dimensional struc.pdf
What are the advantages for proteins to form three-dimensional structures using non-covalent
(weak) interactions?
Solution
PROTEIN FOLDING MODELS:
1. Frame work model:
In this the protein local elements which are stretches of amino acids liked by one another by
covalently with peptide bonds. The region of the primary amino acids sequence in peptide bonds
makes different domains. In these domains some of regions are making with Alfa helix and some
are beta sheet domains. These primary elements form secondary structure independently of
tertiary structure (kim and baldwin).these elements can diffuse un till they collided, successfully
adhering and coalescing to give the tertiary structure (diffuse-collision model),(karplus and
weaven).
2. The classic nucleation model:
It postulates that some neighboring residues in the sequence would form native secondary
structure that would act as a nucleus form which the native structure would propagate in a step
wise manner. Thus the tertiary structure would form as necessary consequence of the secondary
structure (wetlaufer).
3. Hydrophobic collapse model:
It is hypothesized that a protein would collapse rapidly around its hydrophobic side chain and
then arrange from restricted conformational space occupied by the intermediate. Here the
secondary structure would be directed by native like tertiary structure (ptitsyn & kwajima).
Leviathan’s paradox:
It is formulated by Cyrus Leviathan. There are vast too many different possible conformations
for a protein to fold by a random search.
Structural organization of protein:
1. Primary Structure: It refers the sequence of amino acids along with the disulphide bonds.
2. SECONDARY STRUCTURE:
Alfa- Helices and Beta-Pleated sheets are most frequently occurring in secondary structure in
polypeptides. Both of these can case local folding of protein.
the Alfa - Helices in polypeptide made up of L Alfa amino acids are right handed, the - Helices is
stabilized by hydrogen bonds formed between oxygen and amide hydrogen’s of peptide bonds
that are a part of linear sequence.
Beta-Pleated sheets: 2 types
A. Parallel: in this the adjacent hydrogen bonding segments are connected by cross over
connection [Right handed].
B. Anti-Parallel: In this the adjacent hydrogen bonding segments are connected by HAIRPIN
turns or reverse turn [Left Handed].
3. Tertiary structure:
It is arisen because of the folding of poly peptides upon itself.
4. Quaternary structure:
Some proteins are made up of 2 or more polypeptides chains, the interaction between different
poly peptide are subunits gives rise to the quaternary structure.
Non-covalent (weak) interactions advantages in proteins:
In proteins mainly 4 types of non-covalent interactions are present.
1. Hydrophobic region R-CH3 ------- H 3 C-R
2. H-bonding between R-group G-OH ------ N=R
3. Salt bridge R-COO------ NH 3 -R
4. Van der Waals force
The non-covalent bonds, which are present between the peptides, can forms interactions between
indivi.
7.5 proteins2
The document discusses the four levels of protein structure - primary, secondary, tertiary, and quaternary. It explains the significance of each level. The primary structure is the sequence of amino acids. The secondary structure involves hydrogen bonding that forms alpha helices and beta sheets. Tertiary structure describes the overall 3D shape formed by interactions between secondary structures. Quaternary structure refers to complexes of multiple polypeptide chains. The document also discusses membrane proteins and the roles of polar and non-polar amino acids in protein structure and function.
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Proteins fold. How WhySolutionANSProtein folding Protein.pdf
Proteins fold. How? Why?
Solution
ANS:
Protein folding: Proteins are the molecules in the body which carries out many important
functions, such as enzymes and antibodies.
Before proteins carry out their function, they must first assemble themselves or fold.
PROTEIN FOLDING MODELS:
1. Frame work model:
In this the protein local elements which are stretches of amino acids liked by one another by
covalently with peptide bonds. The region of the primary amino acids sequence in peptide bonds
make different domains.in this domains some of regions are made with Alfa - helix and some are
beta sheet domains.
These primary elements form secondary structure independently of tertiary structure (kim and
baldwin).these elements can diffuse until they collided, successfully adhering and coalescing to
give the tertiary structure (diffus-collision model), (karplus and weaven).
2. The classic nucleation model:
It postulates that some neighboring residues in the sequence would form native secondary
structure that would act as a nucleus form which the native structure would propagate in a step
wise manner. Thus the tertiary structure would form as necessary consequence of the secondary
structure (wetlaufer).
3. Hydrophobic collapse model:
It is hypothesized that a protein would collapse rapidly around its hydrophobic side chain and
then arrange from restricted conformational space occupied by the intermediate. Here the
secondary structure would be directed by native like tertiary structure (ptitsyn & kwajima).
Leviathal’s paradox:
It is formulated by Cyrus Leviathal. It explains, there are vast too many different possible
conformations for a protein to fold by a random search.
Structural organization of protein:
1. Primary Structure: the sequence of amino acids along with the di sulphide bonds.
2. SECONDARY STRUCTURE:
Alfa Helices and Beta- Pleated sheets are most frequently occur in secondary structure in
polypeptides. Both of these can case local folding of protein.
The Alfa Helices in polypeptide made up of L- Alfa amino acids are right handed, the Alfa -
Helices is stabilized by hydrogen bonds formed between oxygen and amide hydrogen’s of
peptide bonds that are a part of linear sequence.
Beta- Pleated sheets: 2 types
A. Parallel: in this the adjacent hydrogen bonding segments are connected by cross over
connection [Right handed].
B. Anti-Parallel: In this the adjacent hydrogen bonding segments are connected by HAIRPIN
turns or reverse turn [Left Handed].
3. Tertiary structure: It is arisen because of the folding of poly peptides upon itself.
4. Quaternary structure:
Some proteins are made up of 2 or more polypeptides chains, the interaction between different
poly peptide are subunits gives rise to the quaternary structure..
What are the advantages for proteins to form three-dimensional struc.pdf
What are the advantages for proteins to form three-dimensional structures using non-covalent
(weak) interactions?
Solution
PROTEIN FOLDING MODELS:
1. Frame work model:
In this the protein local elements which are stretches of amino acids liked by one another by
covalently with peptide bonds. The region of the primary amino acids sequence in peptide bonds
makes different domains. In these domains some of regions are making with Alfa helix and some
are beta sheet domains. These primary elements form secondary structure independently of
tertiary structure (kim and baldwin).these elements can diffuse un till they collided, successfully
adhering and coalescing to give the tertiary structure (diffuse-collision model),(karplus and
weaven).
2. The classic nucleation model:
It postulates that some neighboring residues in the sequence would form native secondary
structure that would act as a nucleus form which the native structure would propagate in a step
wise manner. Thus the tertiary structure would form as necessary consequence of the secondary
structure (wetlaufer).
3. Hydrophobic collapse model:
It is hypothesized that a protein would collapse rapidly around its hydrophobic side chain and
then arrange from restricted conformational space occupied by the intermediate. Here the
secondary structure would be directed by native like tertiary structure (ptitsyn & kwajima).
Leviathan’s paradox:
It is formulated by Cyrus Leviathan. There are vast too many different possible conformations
for a protein to fold by a random search.
Structural organization of protein:
1. Primary Structure: It refers the sequence of amino acids along with the disulphide bonds.
2. SECONDARY STRUCTURE:
Alfa- Helices and Beta-Pleated sheets are most frequently occurring in secondary structure in
polypeptides. Both of these can case local folding of protein.
the Alfa - Helices in polypeptide made up of L Alfa amino acids are right handed, the - Helices is
stabilized by hydrogen bonds formed between oxygen and amide hydrogen’s of peptide bonds
that are a part of linear sequence.
Beta-Pleated sheets: 2 types
A. Parallel: in this the adjacent hydrogen bonding segments are connected by cross over
connection [Right handed].
B. Anti-Parallel: In this the adjacent hydrogen bonding segments are connected by HAIRPIN
turns or reverse turn [Left Handed].
3. Tertiary structure:
It is arisen because of the folding of poly peptides upon itself.
4. Quaternary structure:
Some proteins are made up of 2 or more polypeptides chains, the interaction between different
poly peptide are subunits gives rise to the quaternary structure.
Non-covalent (weak) interactions advantages in proteins:
In proteins mainly 4 types of non-covalent interactions are present.
1. Hydrophobic region R-CH3 ------- H 3 C-R
2. H-bonding between R-group G-OH ------ N=R
3. Salt bridge R-COO------ NH 3 -R
4. Van der Waals force
The non-covalent bonds, which are present between the peptides, can forms interactions between
indivi.
7.5 proteins2
The document discusses the four levels of protein structure - primary, secondary, tertiary, and quaternary. It explains the significance of each level. The primary structure is the sequence of amino acids. The secondary structure involves hydrogen bonding that forms alpha helices and beta sheets. Tertiary structure describes the overall 3D shape formed by interactions between secondary structures. Quaternary structure refers to complexes of multiple polypeptide chains. The document also discusses membrane proteins and the roles of polar and non-polar amino acids in protein structure and function.
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I am Albert J. I am a Microbiology Assignment Expert at nursingassignmenthelp.com. I hold a Masters’ in Microbiology, from La Trobe University, Australia. I have been helping students with their assignments for the past 8 years. I solve assignments related to Microbiology.
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61020161Copyright © The McGraw-Hill Companies, Inc. .docx
6/10/2016
1
Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.
Chapter 3
Molecules
Of Life
3.1 Building Big Molecules
Carbon can share electrons with as
many as FOUR other atoms
Organisms consist mainly of oxygen,
hydrogen, and carbon
3-2
Macromolecules
Carbohydrates, lipids, proteins, and nucleic acids
are called macromolecules because of their large
size
The largest macromolecules are polymers
because they contain many subunits called
monomers that are connected to each other.
3-3
6/10/2016
2
3.2 Proteins
Important for structure and
function
50% of dry weight of most
cells
Several functions
Some proteins are
enzymes
all enzymes are proteins
enzymes increase the rate
of a reaction
Support
Keratin, collagen
3-4
Proteins cont.
Contractile
muscle cells use protein to
contract
Transport
channels, carriers, hemoglobin
Defense
antibodies and clotting
proteins
Some hormones are proteins
insulin, growth hormone
3-5
Amino Acids
Proteins are macromolecules with amino acid
subunits
20 different amino acids
Identical backbones
Different side chains (R group)
Peptide bonds (covalent bonds) hold the amino acids
together
3-6
6/10/2016
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Amino acid diversity.
Variety
is due to
the R
group
3-7
Protein Structure
& Shape
Primary structure
order of amino acids
Secondary structure
coiled or folded shape
hydrogen bonds
between negative
C=O and positive N-H
groups
Protein Shape 2 Tertiary structure
further folding and
bending into globular
and fibrous shapes
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polypeptide chains
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structure such as
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6/10/2016
4
Denaturation Denaturation -
the irreversible
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protein shape
caused by heat
or pH
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structure
enzyme can no
longer function
3-10
Protein Structure
Determines Function
Proteins must have the
correct shape for them to
function.
Enzymes have a shape that
is specific for a given
molecule.
They must fit each other
like a key in a lock.
The protein must be made
right for it to take its final
shape correctly. 13-11
3.3 Nucleic Acids
These are long chains of
nucleotides
Nucleotides are made of
a sugar, a nitrogen-
containing base, and a
phosphate
DNA – deoxyribonucleic acid
The genetic material
RNA – ribonucleic acid
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make proteins
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6/10/2016
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5.6 ATP: The Energy
Currency of the Cell, pg 100
Adenosine
Triphosphate (ATP)
A nucleotide with the
base adenine and the
sugar ribose making a
compound adenosine
Is broken down to
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diphosphate (ADP)
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3-14
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gluco.
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Protein metabolism and nitrogen fixation and metabolism
- The document discusses protein metabolism and nitrogen fixation. It covers the classification of proteins based on their structure, composition, and functions. There are four levels of protein structure - primary, secondary, tertiary, and quaternary.
- The primary structure is the linear sequence of amino acids. The secondary structure involves folding into alpha helices or beta sheets via hydrogen bonding. Tertiary structure describes the overall 3D shape formed by interactions between amino acid R groups. Quaternary structure applies to proteins with multiple polypeptide chains that combine to form complexes.
- Proteins are classified as globular, fibrous, or intermediate based on their shape. They can also be simple or conjugated based on composition
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QUESTION 10
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Attachment factors are essential for viral infection
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Attachment factors facilitate the binding of the virion to the entry receptor
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Any young healthier individual that had varicella before is at a high risk of developing herpes zoster
Any old individual is at a high risk of developing herpes zoster even if have never been infected with Varicella-zoster virus
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61020161Copyright © The McGraw-Hill Companies, Inc. .docx
6/10/2016
1
Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.
Chapter 3
Molecules
Of Life
3.1 Building Big Molecules
Carbon can share electrons with as
many as FOUR other atoms
Organisms consist mainly of oxygen,
hydrogen, and carbon
3-2
Macromolecules
Carbohydrates, lipids, proteins, and nucleic acids
are called macromolecules because of their large
size
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because they contain many subunits called
monomers that are connected to each other.
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6/10/2016
2
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function
50% of dry weight of most
cells
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Some proteins are
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all enzymes are proteins
enzymes increase the rate
of a reaction
Support
Keratin, collagen
3-4
Proteins cont.
Contractile
muscle cells use protein to
contract
Transport
channels, carriers, hemoglobin
Defense
antibodies and clotting
proteins
Some hormones are proteins
insulin, growth hormone
3-5
Amino Acids
Proteins are macromolecules with amino acid
subunits
20 different amino acids
Identical backbones
Different side chains (R group)
Peptide bonds (covalent bonds) hold the amino acids
together
3-6
6/10/2016
3
Amino acid diversity.
Variety
is due to
the R
group
3-7
Protein Structure
& Shape
Primary structure
order of amino acids
Secondary structure
coiled or folded shape
hydrogen bonds
between negative
C=O and positive N-H
groups
Protein Shape 2 Tertiary structure
further folding and
bending into globular
and fibrous shapes
Quaternary structure
associations of two
or more separate
polypeptide chains
only some proteins
have a quaternary
structure such as
hemoglobin
6/10/2016
4
Denaturation Denaturation -
the irreversible
change of
protein shape
caused by heat
or pH
causes the loss
of 2o and 3o
structure
enzyme can no
longer function
3-10
Protein Structure
Determines Function
Proteins must have the
correct shape for them to
function.
Enzymes have a shape that
is specific for a given
molecule.
They must fit each other
like a key in a lock.
The protein must be made
right for it to take its final
shape correctly. 13-11
3.3 Nucleic Acids
These are long chains of
nucleotides
Nucleotides are made of
a sugar, a nitrogen-
containing base, and a
phosphate
DNA – deoxyribonucleic acid
The genetic material
RNA – ribonucleic acid
A copy of DNA used to
make proteins
3-12
6/10/2016
5
5.6 ATP: The Energy
Currency of the Cell, pg 100
Adenosine
Triphosphate (ATP)
A nucleotide with the
base adenine and the
sugar ribose making a
compound adenosine
Is broken down to
release energy and
form adenosine
diphosphate (ADP)
3-13
3.4 Carbohydrates
3-14
Used as an immediate
energy source
Hydrophilic molecules
Simple sugars
Major monosaccharides
gluco.
Protein & amino acid (ulivina pratini)
This document discusses amino acids and proteins. It begins by defining proteins as polymers of amino acids and describing the basic structure of amino acids. It then covers the different configurations of amino acids, their properties in aqueous solutions, and classifications. The document also discusses the structures of peptides and proteins at the primary, secondary, tertiary, and quaternary levels. It describes the digestion and metabolism of amino acids as well as the urea cycle. Finally, it provides an overview of protein biosynthesis, including the roles of DNA, mRNA, tRNA, and ribosomes.
Proteins & amino acids (ulivina pratini)
This document discusses amino acids and proteins. It begins by defining proteins as being formed from amino acids, which are the monomers or building blocks of proteins. The document then covers the structure of amino acids, including their general formula and configurations. It also discusses the properties of amino acids in aqueous solutions and their classification as essential or non-essential. The document goes on to explain how amino acids can bond together to form peptides and polypeptides, and the levels of protein structure from primary to quaternary. It concludes with sections on the metabolism of proteins and amino acids in the body.
integral membrane protein.pdf
This document discusses membrane proteins and their structure. It begins by defining membrane proteins and their classification based on interaction with membranes and cellular location. It then discusses the different types of membrane proteins in detail, including integral/intrinsic proteins that strongly interact with membranes and peripheral/extrinsic proteins that interact weakly. It also covers the primary, secondary, tertiary, and quaternary structure of membrane proteins. In particular, it notes that most membrane proteins form alpha helices to span the hydrophobic interior of membranes, and that helices associate through interactions between polar residues and helical moments.
Protein structural organisation
Proteins play key roles in living systems through catalysis, transport, and information transfer. They have a hierarchical structure including primary, secondary, tertiary, and quaternary levels. The primary structure is the amino acid sequence, and higher levels of organization are determined by the primary structure. Protein folding and interactions between residues determine the final 3D tertiary and quaternary structures, which are critical for protein function. Misfolded proteins can cause diseases.
Protein structure classification/domain prediction: SCOP and CATH (Bioinforma...
This pdf is about the protein structure classification/domain prediction: SCOP and CATH (Bioinformatics).
For more details visit on YouTube; @SELF-EXPLANATORY;
https://www.youtube.com/channel/UCAiarMZDNhe1A3Rnpr_WkzA/videos
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online chemistry exam help
I am Gevorgyan A.. I am an Online Chemistry Exam helper at liveexamhelper.com. I hold a master' Degree in Chemistry from the University of Denver, USA. I have been helping students with their exams for the past 8 years. You can hire me to take your exam in Online Chemistry. Visit liveexamhelper.com or email info@liveexamhelper.com. You can also call on +1 678 648 4277 for any assistance with the Online Chemistry Exam.
Overview of Systems Microbiology: Sample Assignment Solutions
I am Thomas Sutton, an expert in Biology assignments at biologyassignmenthelp.com, with a Ph.D. in Biology from Northwestern University. With 9 years of experience, I specialize in Systems Microbiology assignments. For assistance, visit biologyassignmenthelp.com, email info@biologyassignmenthelp.com, or call +1 315 557 6473. This sample assignment solutions include detailed analyses of microbial interactions within ecosystems, highlighting key biochemical pathways and their environmental impacts.
Protein structures by amina
Proteins have four levels of structure:
1) Primary structure is the linear sequence of amino acids in the polypeptide chain held together by peptide bonds.
2) Secondary structure involves the local 3D structure of portions of the chain, forming alpha helices or beta sheets.
3) Tertiary structure describes the overall 3D structure of a single polypeptide chain, including side chains.
4) Quaternary structure refers to the 3D arrangement of multiple polypeptide subunits that make up a single protein.
Protein Folding
This document discusses protein structure and folding. It describes the four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the amino acid sequence. Secondary structure involves folding into alpha helices or beta sheets. Tertiary structure is the overall 3D shape formed by interactions between amino acid side chains. Quaternary structure refers to interactions between multiple polypeptide chains in a protein. The document also discusses protein folding, denaturation, and misfolding, noting that many neurodegenerative diseases are associated with misfolded protein aggregates.
2.4 & 7.3 Notes
Guided notes covering material from Topics 2.4 and 7.3 of the updated IB Biology syllabus for 2016 exams. Notes sequence and prompts are based on the Oxford IB Biology textbook by Allott and Mindorff.
Protein folding
The document discusses protein folding, which is the process by which a polypeptide chain folds into its characteristic and functional three-dimensional structure. It describes the four levels of protein structure: primary, secondary, tertiary, and quaternary. Key drivers of folding are the hydrophobic effect and formation of hydrogen bonds. Chaperone proteins assist in protein folding in vivo. Factors such as mutations, errors in synthesis, environmental stresses, and aging can cause proteins to misfold and aggregate, which is associated with various diseases. Cells use molecular chaperones and protein degradation systems to prevent aggregation, but these become less effective with age.
12 miller chap.3 lecture
The document discusses the hierarchical structure of proteins from primary to quaternary structure. It explains that a protein's amino acid sequence determines its 3D tertiary structure and function. The document also covers protein folding, common structural motifs, examples of protein function like enzymes and ligand binding proteins, and how chaperones assist in protein folding. It discusses how proteins evolve into families and provides examples of structural similarities between protein homologs like globins.
IB Biology 2.4 & 7.3 Slides: Proteins
Slides covering material from Topic 1.2 (and some AHL material from 7.3) of the updated IB Biology syllabus for 2016 exams
Chemistry hl human biochemistry option self study guide
This document outlines a self-directed study guide for the Chemistry HL Human Biochemistry Option. It lists learning objectives that cover topics including: calculating energy from combustion data; drawing amino acid structures; describing protein structure and analysis; comparing carbohydrate structures; distinguishing lipids; outlining micronutrients and macronutrients; describing enzyme function; and comparing aerobic and anaerobic respiration. The guide provides resources for students to research topics and complete related worksheets to check understanding.
Bio110 practice problems chap3 part3
1. Proteins in biological systems may be enzymes that catalyze reactions.
2. The functional groups of amino acids may be hydrophobic or hydrophilic.
3. A new amino acid containing only hydrogen and carbon atoms in its R-group would be predicted to be hydrophobic relative to amino acids found in organisms.
1.3 Membrane Structure
The document discusses membrane structure. It describes how phospholipids form bilayers in water due to their amphipathic properties. The hydrophilic head of phospholipids is attracted to water, while the hydrophobic tail is repelled by water. This allows phospholipids to orient themselves with heads facing the water and tails facing each other, forming bilayers or micelles. Cholesterol is also discussed, and how it reduces membrane fluidity. Membrane proteins, glycoproteins, and their various functions are briefly covered. Early models of membrane structure are mentioned, such as the Davson-Danielli model which was later replaced by the fluid mosaic model.
2009 CSBB LAB 新生訓練
The document discusses protein structure concepts and related computational problems. It covers what proteins are made of, including amino acids, peptides, and protein structure levels from primary to quaternary. It also discusses protein domains, structural databases like PDB and SCOP, and principles of structural alignment and superimposition to identify structural similarities between proteins.
Protein metabolism and nitrogen fixation and metabolism
- The document discusses protein metabolism and nitrogen fixation. It covers the classification of proteins based on their structure, composition, and functions. There are four levels of protein structure - primary, secondary, tertiary, and quaternary.
- The primary structure is the linear sequence of amino acids. The secondary structure involves folding into alpha helices or beta sheets via hydrogen bonding. Tertiary structure describes the overall 3D shape formed by interactions between amino acid R groups. Quaternary structure applies to proteins with multiple polypeptide chains that combine to form complexes.
- Proteins are classified as globular, fibrous, or intermediate based on their shape. They can also be simple or conjugated based on composition
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CHUYÊN ĐỀ ÔN TẬP VÀ PHÁT TRIỂN CÂU HỎI TRONG ĐỀ MINH HỌA THI TỐT NGHIỆP THPT ...
Creative Restart 2024: Mike Martin - Finding a way around “no”
Creative Restart 2024: Mike Martin - Finding a way around “no”
Question 8- A-) Protein structure- Describe how the following two inte.docx
- 1. Question 8. A.) Protein structure. Describe how the following two interactions are critical in protein structure: (i) hydrogen bonds between backbone atoms in the formation of secondary structure elements, and (ii) hydrophobic side chains in the formation of the hydrophobic core of a protein. In your answer explain the chemical structure of the protein backbone, describe hydrogen bonding in alpha-helices and beta-sheets, and explain the difference between hydrophilic and hydrophobic amino acids. B.) Protein families . Describe (i) how the process of molecular evolution generates protein families, and (ii) how the amino acid sequence alignments based on sequence similarities for such members of a protein family can be used to identify conserved regions of a protein and construct a phylogenetic tree of such members of a protein family. (iii) Will amino acids at the active site of an enzyme tend to be conserved in a protein family? Why? C.) Protein evolution. (i) Illustrate the phenomenon of functional sequence variation using antibodies that can bind to a range of different antigens. (ii) Explain the process of domain shuffling in protein evolution and give an example of how this process can generate proteins with novel functions.