Book Identity Book I
Book Identity Book I
Book Identity Book I
INTRODUCTION
Book Identity
Book I
Title book : Fundamental Molecular Biology
Author : Lizabeth A. Allison
Publisher : Blackwell Publishing Ltd
Publication Year : 2007
Printing : Thirteen
Dimensional book : Soft copy
Page the book review : 85-107
No. ISBN : 978-1-4051-0379-4
Book II
Book II
Protein constitue most of cells dry mass. They are not only the cell
building block; they also execute nearly all the cells functions, Thus, enzymes
provide the intricate moleculer surface in cell that promote its many chemical
reaction. From a chemical point of view, protein are by far the most structurelly
complex and functionally sophisticated moleccules known. There are 20 types of
amino acids in protein, each with different chemical properties. A protein
molecules is made from a long chain of those amino acids that linked together to
neighbor through covalent peptide bond. The repeating sequence of atoms along
the core of polypeptide chain reffered to as the polypeptide backbone, attached the
amino acids side chains.
Globular regions, known as domains, are the modular units from which
many proteins are constructed; such domains generally contain 40-350 amino
acids. small proteins typically consist of only a single domain, while large
proteins are formed from several domains linked together by various lengths of
polypeptide chain, some of which can be relatively disordered. As proteins have
evolved, domains have been modified and combined with other domains to
construct new proteins. Thus far, about 800 different ways of folding up a domain
have been observed, among more than 20,000 known protein structures.
Proteins are brought together into larger structures by the same
noncovalent forces that determine protein folding. Proteins with binding sites for
their own surface can assemble into dimers, closed rings, spherical shells, or
helical polymers. Although mixtures of proteins and nucleic acids can assemble
spontaneously into complex structures in a test tube, many biological assembly
processes involve irreversible steps. Consequently, not all structures in the cell are
capable of spontaneous reassembly after they haue been dissociated into their
component parts.
Proteins reversibly change their shape when ligands bind to their surface.
The allosteric changes in protein conformation produced by one ligand affect the
binding of a second ligand, and this linkage between two ligand-binding sites
provides a crucial mechanism for regulating cell processes. Metabolic pathways,
for example, are controlled by feedback regulation: some small molecules inhibit
and other small molecules activate enzymes early in a pathway. Enzymes
controlled in this way generally form symmetric assemblies, allowing cooperetive
conformational changes to create a steep response to changes in the concentrations
of the ligands that regulate them.
Book III
Proteins are linear polymers of amino acids linked together by peptide
bonds. A protein can have a single polypeptide chain or multiple polypeptide
chains. Protein are polymers constructed out of 20 different types of amino acids.
Individual amino acids are linked together in linear, unbranched chains by
covalent amino bonds called peptide bonds. Peptide bonds formation between the
amino group of one amino acid and the carboxyl group of another results in the
net release of water molecules and thus is a form of dehydration reaction. The
primary structure of a polypeptide chain is the sequence of covalently linked
amino acids that compose the chain. Various, mosrly noncovalent interactions
between amino acids in the linear sequence stabilize a protein's specific folded
three-dimensional structure, or conformation.
The helix, strand and sheet, and 13 turn are the most prevalent
elements of protein secondary structure. Secondary structures are stabilized by
hydrogen bonds between atoms of the peptide backbone. Protein tertiary structure
results from hydrophobic interactions between nonpolar side groups and hydrogen
bonds and ionic interactions involving polar side groups and the polypeptide
backbone. These interactiom; rabilize folding of the protein, including its
secondary structural elements, into an overall three-dimensional arrangement.
Certain combinations of secondary structures give rise to different structural
motifs, which are found in a variety of proteins and are often associated with
specific functions.
Albert Books too has a good linkage one becouse the arragement of
core content are appropriate with the molecular generally about protein
structure and function topic. This books start with introduction of protein,
shape and structure of proteins, the shape of a protein is specified by its
amino acid sequence, proteins fold into a conformation lowest energy, the
helix and sheet as component of structure, protein domains, protein
classified, summary and function with clearly explanation in every function.
In this book has use more complicated word that means well found a bit little
terminology or latin greek and more of figure and table that support the
explanation before. This books actually can already use for student who want
to mastery the molecular with a little bit deeper.
Lodish books too has a good linkage becouse like the lizabeth and
alberts books the arragement composistion of contant are appropriate with
the standart generally. There are start with the introduction of protein,
hierachical structure of proteins, protein folding, protein binding and enzyme
catalysis, regulating protein function, purifying, and characterizing protein
and last is proteonimcs. Explanation of this book are more better than 2 book
before becouse the contant completed, proved of the statement based on
experience and experiment, in this book consist more greek latin than alberts
and elizabeth and all of sub topic linkage so we need higher order thinking to
understand clearly about concept or theory inside.
b. Curretness
Lizabeth books has the good figures or picture, and every figures or
picture has good and clear explanation to make easy if we learn of book.
Example for explanation of the structure protein and component inside the
structure are clearly and easy to understand for beginners with a complete
description bellow the figure.
Alberts books has the better good than lizabeth content of figure or
anything else. When we read this book then compared to many journal
international had been publish, the content has verify.
Lodish books has the more better good than alberts and lizabeth books
becouse this book write based on experiment or journal publishing. And
word selection are suitable for thinking more by her-self or independent
learner. So that this books really responsibility for author or reader.
Book Weakness
a. Linkage between chapter
Generally Lizabeth book has good linkage between subtopic, but there are
the weakness, it can be seen when this book explain about the quaternary struture
of protein, the figure are present but its not enough to make reader imanging how
the form of this struture, then figure of the componet of queternary structure also
lack. And next in sub-title that discus about protein contain multiple functional
domain author also not using the figure to clear the explanation. Its make the
readers not easy to understand the meaning every paragraf cause we know that the
matter of this a bit complicated. As long as i read the books of albert and lodish i
cant found the weakness linkage becouse the linkage are complated based on
standar composition of this topic. Author has arranged with good one.
b. Currentness
The content this book has lack the explanation about materi for
learning or have generally expalanation if we compare with Alberts and
lodish book, Alberts and lodish book have specific explanation from the
molecular side
Implication
a. Implication to the theory/concepts
The three books has the good theory/concepts about the protein
structure and function becouse each book start with the introduction the
protein, meaning of protein, characteristic generally, component
arrangement inside, structure of protein: primary structure, seccondary
structure, tertiary structure, and quarternary structure, summary, function
of protein with details explanation every function, and if we compare one
each other actually right well found the different of them but just a little
bit. The completed one of explanation or arragement theory and concepts
actually found in Lodish books beccouse in this book after theories author
put down the experiment observation to prove it. But its not to said that
other book is bad, Lodish book is relevant to people that want to mastery
olecular protein with deeper. and for lizabeth and alberts books are suitable
for student or people that want to learn about molecular protein in
generally.
b. The developments program in Indonesia
If we compare the three books with indonesian books of course its
was different, becouse in the painful fact that indonesian book mostly
copy paste from one to another one and most of them has lack of figure to
complete the explanation. Then rarely use any journal as the reference of
the statement inside the book or put down the experiment to prove that.
But maybe thislizabeth, Lodish and Albert books can make references for
indonesia book to introducced the protein structure and function topic and
maked easy to know the protein topic.
Protein chapter that dicuss in the three books are correctly same
with journal international that publishing so that its means the content has
verify and its can help student or people in indonesia who want to learn
about protein as molecular object in completed, coordinates, and easy
ways with them-self or independent ways. The book should be as students
source to look for information related to the protein from molecular view
aspect for their study as well as Indonesian curriculum.
Suggestion
Maybe Lizabeth book can make the specific and more expalanation about
protein function and structure especially in molecular biologi course, then addd
more figure and table explanation about the topic as albert and lodish do in their
books.
REFERENCES
Anil Kumar Mandle, Pranita Jain, And Shailendra Kumar Shrivastava. 2012.
Protein Structure Prediction Using Support Vector Machine. India:
International Journal On Soft Computing (Ijsc) Vol. 3
Bruce Alberts, Alexander Johnson, Julian Lewis, Martin Raff, Keith Roberts,
Peter Walter. 2008. Molecular Biology of the Cell Fifth Edition.
United States America: Garland Sience, Taylor & Francis Group and
etc, 81-150.
Harvey Lodish, Arnold Berk, Chris A. Kaiser, Monty Krieger, Anthony Bretscher,
Hidde Ploegh, Angelika Amon, Matthew P. Scott. 2013. Molecular
Cell Biology Seventh Edition. New York: Katherine Ahr Parker, 59-
114.
Steve Fairchild, Ruth Pachter, And Ronald Perri.2017. Protein Structure Analysis
And Prediction. New York: Wright Laboratory, J. Mol. Bio.