The History Of Molecular Modeling Biology Essay

The History Of Molecular Modeling Biology Essay Molecular modeling is a collection of science and art that study molecular structure and function by using computational technique to generate a realistic model of molecule based on molecular properties and behavior. A special computer graphics application and viewer is required to study the image of molecular structure and chemical process. Normally, molecular modeling is applied in field that related to drug design and computational biology who focus on study of molecular structure, dynamic, properties, biological activity (e.g. protein folding, protein stability, protein recognition, and structure prediction, structure determination), and new molecular system design. This is because modeling can support a systematic way to investigate the molecular structure, flexibility and function. The computational approach that used in molecular modeling consists of molecular mechanic, quantum mechanics, and molecular simulation. Molecular mechanic is based on empirical result to model the molecular system through motion of an object. For instance, potential energy is calculated by using force field method. Quantum mechanics is described by using wave function and it is important for understand how the atoms are covalently combine to form molecule. Its example is ab initio and semi-empirical quantum mechanics. Molecular simulation is another computational technique which includes molecular dynamics and Monte Carlo. However, to date, molecular modeling is more concerns to the use of a variety of methods to deduce the atomic information of a system which includes all the approaches mentioned above. To know more about molecular modeling, we are advised to know some of its history so we can make sense of molecular modeling as we know it today. In 1858, Archibald Scott Couper, Friedrich August Kekulà © von Stradonitz, and Aleksandr Mikhailovich Butlerov introduced chemical structure with a structure rule that involves the link of carbons and other atoms. Louis Pasteur modified the molecular structure theory in 1860. In 1865, August Wilhelm Hofmann discovered ball and stick model and color scheme. And Alder and Wainwright performed simulation technique on hard spheres model in 1959. Lifson, Scheraga, Allinger, Levitt, Warshel and others introduced the force field concept in 1960. Whilst in 1970, Rahman and Stillinger described the molecular dynamic simulation of water. In 1971, Protein Data Bank (PDB) was established. In 1977 and 1984, water force field was developed by Berendsen and Jorgensen respectively. At same year, Warshel and colleagues published the concept of protein elec trostatics and enzyme-substrate complex. At late 1980s, high speed computer, program, technology innovation, and a variety of algorithm were introduced. From paragraph above, we only know some important year between late 1850s to 1980s. From 1970s onwards, there is a proposed expectation curve as shown in Figure 1.1. As computational method and technology are more available, the expectation towards biomolecular modeling field was continued to rise especially from 1980s to 1990s. Structure based rational drug design was then introduced. It was expected to replace the less efficient methods. However, unrealistically disappointment was followed. Then scientists undergo a recovery phase where Human Genome Project was introduced and new technology with fast workstation was published. With these, a steady progress of productivity is emerged until today in order to reach the realistic expectation. In addition, it is important to know that the latest molecular modeling trend is focusing on the development and implementation of virtual reality whose enhance the three dimensional visualization. Nowadays, molecular modeling has been altered the way to conduct a research, that is choosing the experiment with highest probability of success before perform it. So, there is a demand to have a better and faster program design. It is important to know that molecular model need not be commercial or costly to prepare, inexpensive materials also possible to produce useful model and result. Question 2: Molecular graphics and molecular viewer If we said that molecular modeling is creation of computational model based on molecular properties and behavior, then molecular graphic is the graphical depiction of molecular modeling. Molecular graphic is a discipline of study molecule through visualization of molecules and their component parts. It is refers to three-dimensional depictions of molecules that made to examine and understand their response during reaction and interaction. To date, molecular graphic has been replaced some function of physical molecule model as it is portability and easy to interact with analysis result. In the early stage of molecular graphic, computer graphic tool was dominated by vector graphical representation based on calligraphic technology. During that time, only line and dot were shown. And main frame computer was required to manipulate the molecular structure before submit to graphic hardware. Until the founded of Molecular Graphics Society (known as Molecular Graphics and Modeling Society today) in 1983 and present of Journal of Molecular Graphics, new graphic techniques, hardware device and graphical software were introduced. This discovery allows the interactivity on the basis of space filling molecular model. As we know that, molecular objects are in three-dimensional structure. So molecular graphic representation (MGR) is concerns to the multi-dimensionality in order to provide more molecular information. Graphical excellence is used as a guideline for the MGR development. It is well designed to present data and it consists of complex idea that able to communicate with clarity, precision, and efficiency. Basically, the graphical display will shows data, induces viewer to have greatest number of idea, makes large data set to be coherent, encourage eyeball technique to compare data by using human eye, integrates statistical and verbal description of a data set, and reveals data at different levels to give more details. There are several types of molecular model that relate to molecular graphic in order to combine the computational technique with graphic art. Here, I will briefly discuss a few types that commonly used. Ball and stick model is the most widely used molecular model. It displays the three-dimensional position of atoms and bonds that link between them. Typically, atom is represented by sphere with specific color and bond is represented by rod. The rod can be rotate to provide the insight of bond flexible. The Figure 2.1 shows the proline in ball and stick model and its structural formula. Black color represents carbon, white represents hydrogen, blue represents nitrogen, and red represents oxygen. Stick model (refer Figure 2.2) is similar to ball and stick model but without ball as it represents all atoms and bonds by using rod with different color scheme. Space filling model (refer Figure 2.2) is a type of  three-dimensional  molecular model  where the  atoms  are represented by van der Waals spheres with different color and join directly to one another. Its measurement scale is the same as the real atom scale. It shows the space that atom occupied instead of shows the chemical bond. Wire frame model (refer Figure 2.3) is similar to stick model which shows the connection of atom by different color scheme but with thinner bond (connector). This model is convenient for drawing large molecules. Chicken wire model (refer Figure 2.4) is another method to visualize molecular model by drawing the polygon mesh on surface. Its shape is similar to the regular  hexagonal  pattern with mesh  structure. Ribbon model (refer Figure 2.5) is a three dimensional schematic molecular model that used to represent protein structure. It shows the path and organization of protein backbone, and serves as visual framework that provides details of atomic structure. Coiled ribbon represents ÃŽ ±-helix,  arrow represents ÃŽ ²-strand, and thin tubes represents loop. It shows the visual basic of molecular structure such as twist and fold. Molecular viewer is the molecular graphic software that used to visualize molecular structure. It is selected based on the size of molecule and the task to do. Here, I will briefly discuss a few types of viewer that commonly used. RasMol is a powerful research tool for visualization of protein, nucleic acid, and small molecules. It is easy to use while able to produce high quality three-dimensional image. It is a free viewing system for PDB coordinate files. Chime is a molecular viewer that modified RasMol code to allow visualization of molecule through web browser. It able to display three-dimensional and interactive molecular model from webpage. Jmol is a Java-based molecular viewer that allows visualization of molecule through web browser (like Chime) or stand-alone computer (like RasMol). It supports many different source files such as PDB format to create molecular model. Cn3D is NCBIs three-dimensional structure viewer. It allows the display of three-dimensional structure, sequence, and sequence alignment with annotation and alignment editing feature from NCBIs Entrez. Swiss PDB Viewer or DeepView is a molecular viewer that provide user friendly interface which allows analyzing several proteins or multiple models at same time. It supports alignment which based on individual residue, main chain, or entire protein. It also can align different homologous protein structure. It can be used as a helper application for browser. Visual Molecular Dynamics (VMD) is designed for visualization of large structure molecule such as protein and lipid. Except visualization, VMD also can analyze molecular dynamic simulation, act as graphical front end by display and animate molecule, and sequence browsing. Question 3: Protein structure with reference to hemoglobin and the prion protein Protein structure is biomolecular structure of protein molecule which made up of amino acid polymers. It is critical to its activity and biological function. X-ray crystallography  and NMR spectroscopy are technique that used to determine the protein structure. Basically, the complex protein structure is characterized into four levels of organization (refer Figure 3.1). Primary structure of protein is a linear sequence of amino acid structural unit that held together by peptide bond. It is starting from amino terminus (N) and end with carboxyl terminus (C). The sequence of amino acid will determines primary structure of protein. Change in a single position of amino acid will alter the function and activity of protein, some might cause disease. Secondary structure of protein is local conformation of polypeptide chain. It defined by  the pattern of hydrogen bond that formed between peptide backbones. The polypeptide folds locally into stable structure will form alpha helix, beta pleated sheet, and turn conformation. Tertiary structure of protein is a global three-dimensional structure that formed when secondary structures are folded in three-dimensional space. This folding is triggered by hydrophobic interaction and stabilized by hydrogen bond, van der Waal interaction, disulfide bond, and charge-charge interaction. Tertiary structure can be organized by more than one domain. Domain region can be alpha helix, beta sheet or mixed. Tertiary structure refers to each individual domain as well as to the complete configuration of whole protein. Whilst motif is small structure that plays important role in protein prediction. Quaternary structure of protein refers to regular association of more than two polypeptide chains that fold and coil to form a complex. The interaction between subunits can be identical or different. Quaternary structure is known as a stable three-dimensional structure of multi subunit protein. Hemoglobin is example of protein quaternary structure that found in red blood cells who acts as oxygen transport molecule. It carries oxygen from lung to release in tissue, and binds to carbon dioxide in tissue then releases back to lung. This process is characterized by cooperative interaction of polypeptide chains (subunit) by change their structure to make hemoglobin to be properly function. Hemoglobin (Figure 3.2) is an allosteric protein. It is a tetramer that consists of two types of subunits, two ÃŽ ±-chains and two ÃŽ ²-chains that held together by non-polar interaction and hydrogen bond. Each subunit is arranged as alpha helix structural segment and forms a hydrophobic cleft to allow the attachment of a heme  prosthetic group that consists of an iron atom who acts as oxygen binding site. Each of the subunits can carry one molecule of oxygen. Actually, there has no contact between same type of chain, that is alpha-alpha chain, and beta-beta chain. The contact region occurs between alpha-chain and beta-chain such as alpha1beta1  and alpha1beta2. The alpha1beta2  contact region acts as a switch between deoxy (T) structure to the oxy (R) structure. At T structure or tense state, binding of oxygen is difficult. While oxygen is favored at R structure or relax state as binding of oxygen will trigger the affinity of next oxygen to hemoglobin. Transition from T structure to R structure is triggered by stereo chemical changes at the heme group as shown in Figure 3.3. Like other proteins, hemoglobin is created by DNA in body. Alteration of amino acid will cause blood related disorder such as sickle cell anemia. This disease is results from a mutation at sixth residue in the ÃŽ ² hemoglobin monomer. Proteinaceous infectious virion (prion) is an infectious protein that causes neurodegenerative disease such as Scrapie and Bovine Spongiform Encephalopathy (BSE) in mammal, and Creutzfeldt-Jakob (CJD) and Kuru in human. Prion is known as an infectious agent that infects protein, without the transfer of nucleic acid genome, and it causes other proteins to be misfolded. Proteinaceous infectious particle (PrP), a normal cellular protein, consists of around 250 amino acids is found in our body whose involve in the spread of prion disease. Prion theory states that PrP is sole causative agent of prion diseases. If prion is in normal or stable shape (PrPc), it will not cause disease. Whilst if prion is flipped and folded into abnormal conformation (PrPsc), it will cause disease as it induces other proteins to change their conformation and becomes PrPsc as well. This translation is an exponential process where ÃŽ ±-helical and coil structures are refolded into ÃŽ ²-sheet. PrPc  is the endogenous form of prion protein (PrP), while PrPsc  is the misfolded form of PrP. PrPc and PrPsc are known as protein isoform with tertiary structure characteristic. They are categorized as same protein but with different conformation as their folding region is different as shown in Figure 3.4. PrPc contains more ÃŽ ±-helical and coil structure  and PrPsc has more ÃŽ ²-sheet structure. Prion structure is extremely stable. It is highly resistant to denaturation either by heat, ultraviolet light, or radiation. This characteristic makes prion difficult to be eliminated. Furthermore, prion comes in different strains. Each of the strain has slightly different structure. In other words, there has no effective treatment to fight with prion diseases. Question 4: Protein databases Database is an organized collection of data which allows the convenient access of user. Database can be classified into a variety of type. Here, we only focus on the protein data type. There are three types of protein database, that is protein structure database, protein sequence database, and protein motif database. Before discuss the three types of databases, I would like to briefly describe Protein Data Bank (PDB) which is the primary protein database. Protein Data Bank (PDB) is a worldwide repository of three-dimensional structural data of biological macromolecules. Until March 12, 2013, there are 88837 structures in PDB, in which 82224 are protein structure or 92.56% of PDB structure is protein. All the protein structures are obtained through x-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, cryoelectron microscopy (cryoEM), hybrid technique, and other experimental method. Since 1971, PDB is under the management of Bookhaven. Until 1999, Research Collaboratory of Structural Bioinformatics (RCSB PDB) takes over this task. In 2003, Worldwide PDB (wwPDB) maintains and formalizes the international collaboration by involve RCSB PDB (USA), PDB Japan (PDBj), PDB Europe (PDBe), and Biological Magnetic Resonance Data Bank (BMRB) as members of wwPDB. They act as distribution centers of PDB data. PDB acts as a very important resource to organize and share molecule structure data especially in structural biology area. It serves as a global community to allow scientist to share their research. Currently, the newly determined protein structure will be deposited into PDB data before the scientific paper is published. Except three-dimensional database, PDB also known as primary database for protein structure information. Derived or secondary database will use the PDB data and categorize it in a different way based on their own classification. Protein structure database groups protein based on the similar protein structure and common evolutionary origin. Structural Classification of Proteins (SCOP), CATH, and DALI Domain Dictionary (DDD) databases are the three main protein structure classification databases. But here I will only discuss SCOP and CATH. SCOP is a repository that organizes protein structure hierarchically based on their structure and evolutionary origin. The classification of SCOP is manually. With assistant of computer tool, SCOP able to visual and compare the protein structure consistency. The latest version of SCOP is 1.75 that released on June 2009 with 38221 PDB entries and 110800 domains. The source of protein structure is from Protein Data Bank. The classification of SCOP has six levels that are class, fold, superfamily, family, protein, and species. There are eleven classes in SCOP hierarchy which differentiate by fold type: alpha ÃŽ ±, beta ÃŽ ², alpha and beta (ÃŽ ±/ÃŽ ²), alpha plus beta (ÃŽ ±+ÃŽ ²), multi-domain protein, membrane protein, small protein, coiled coil protein, low resolution structure, peptide, and designed protein. Between the eleven classes, only the first seven classes are known as true class and others serve as place holder for protein domain that have not been classified. Proteins are classified into group based on their structure similarity. The unit of classification is protein domain. The shape of domain is known as fold. Proteins share common fold if they have same major secondary structures in same arrangement and same topological connections. Superfamily is probable has common evolutionary origin which share common fold and perform similar function. Family shows a clearly evolutionary relationship of proteins with more than 30% sequence identity. Protein level will connect proteins through similar function and structure. The last level, species, is grouped according to unique sequence. CATH is a semi-automated protein structure classification in which the protein domain is classified based on class (C), architecture (A), topology (T), and homologous superfamily (H). The latest version of CATH is 3.5 that released on September 20, 2011 with 51334 PDB entries, 173536 CATH domains, and 26226 CATH superfamilies. CATH has four classes, they are alpha, beta, alpha and beta, and few secondary structure. The class of protein domain is determined by its secondary structure composition. Architecture level describes the overall shape of domain structure that determined by secondary structure orientation. Then, domain will be grouped into topology level based on secondary structure shape and connectivity. Homologous superfamily level will then grouped protein domains together based on similar structure, function, and has common ancestor. Protein sequence database can be divided into manually and automatically annotated database. UniProtKB/SwissProt and Protein Information Resource-International Protein Sequence Database (PIR-PSD) are example of manually annotated database. UniProtKB/TrEMBL and NCBI GenPept are example of automatically annotated database. Here, I will discuss the UniProt Knowledgebase (UniProtKB) as example. UniProtKB is a protein sequence and functional information database. The data type that captured in is known as protein annotation. UniProtKB consists of two sections: UniProtKB/SwissProt which can be reviewed and UniProtKB/TrEMBL which cannot be reviewed. Most of the sequence in UniProtKB is derived from International Nucleotide Sequence Database (INSD) and some from PDB database. All these sequences will be automatically added into UniProtKB/TrEMBL. Then the TrEMBL records can be manually selected to be integrated into SwissProt record. UniProtKB/SwissProt is a high curated and non-redundant protein sequence database. The release 2013_03 of March 6, 2013 has 539616 sequence entries. It combines the experimental result, computational analysis, and scientific literature in one entry. It provides all relevant information about the searched protein as the sequence form same gene and same species are merged into same entry. Its file format such as FASTA is downloadable by public. UniProtKB/TrEMBL is a high quality computational analyze and redundant protein sequence database. That means, TrEMBL is computer annotated supplement to SwissProt but with multiple entries for sam eprotein. The release 2013_03 of TrEMBL on March 6, 2013 has 32153798 sequence entries. However, its entry is not redundant to SwissProt. Therefore, the entry of UniProtKB on release 2013_03 will be the combination entry of SwissProt and TrEMBL that is 32693414. Protein motif database also known as pattern and profile database is secondary database that derived from conserved pattern obtained from multiple sequence alignment. It is useful for the classification of protein sequence into family level. PROSITE and BLOCKS are example of motif based database. PROSITE is a protein domain, family and functional site database which comprise of biologically significant protein site, pattern, and profile. It analyzes protein sequence for known motif. PROSITE classification is based on observation. Similar protein sequence will be group into family. And protein domain is classified based on families that share common ancestor or has functional attribute. PROSITE records give the information of structure and function for a particular protein. It is part of the  ExPASy  proteomics  analysis servers and it used the annotation of domain features of SwissProt entry. Up to date, the latest version is release 20.91 of March 4, 2013 with 1661 entries, 1308 patterns, 1053 profiles, and 1057 ProRule. ProRule is the case rule that provides extra information about function and structural of critical amino acids. For instance, it contains the information related to biologically meaningful residue such as active sites, co-factor-binding sites,  and post-translational  modification sites. It helps the protein function determination. And it able to generate annotation automatically based on the PROSITE motifs. PROSITE database is used when identify the possible function of newly discovered protein, and determine activity of known protein. We also can derive a signature or conserved sequence from protein in order to classify protein. This is because each PROSITE signature is linked to an annotation document, where has all related information of the particular protein. PROSITE offers tool that can function for motif detection and protein sequence analysis. The most common application or archive is fingerprint that act as evidence to identify an individual. Appendix: Figure 1.1: Expectation curve for biomolecular modeling and simulation File:L-proline-3D-balls.pnghttp://upload.wikimedia.org/wikipedia/commons/thumb/f/ff/Prolin_-_Proline.svg/121px-Prolin_-_Proline.svg.png Figure 2.1: Ball and stick model of proline Structural formula of proline Space filling model Stick modelhttp://www.rsc.org/ej/NJ/2003/b206570n/b206570n-f3.gif Figure 2.2: Stick model (left) and space filling model (right) of proline http://class.fst.ohio-state.edu/FST822/aa/btwf.gif Figure 2.3: Wire frame model http://upload.wikimedia.org/wikipedia/en/thumb/4/4f/DMT_chicken_wire_mesh.png/227px-DMT_chicken_wire_mesh.pnghttp://upload.wikimedia.org/wikipedia/commons/thumb/f/ff/Tubby-1c8z-pymol.png/160px-Tubby-1c8z-pymol.png Figure 2.4: Chicken wire model with stick model Figure 2.5: Ribbon model http://www.piercenet.com/media/ProStructureFig1.gif Figure 3.1: Four levels of protein structure Diagrammatic representation of the structure of hemoglobin Figure 3.2: Hemoglobin http://jr.stryker.tripod.com/images/TransitionRT.jpg Figure 3.3: Conformation transition from T structure to R structure PrPsc PrPcPrion structure Figure 3.4: Prion protein in abnormal conformation, PrPsc (left) and prion protein in normal conformation, PrPc (right)

Honors English- Animal Farm Essay

Fhorest Padilla #209156Padilla 1 Honors English- Animal Farm Essay 2/10/10 The Failure to Improve Society ultimately becomes what it hates the most in order to continually keep moving forward into the future. This is the same for the animals in Animal Farm; they have human aspects in order to give a better understanding even though animals dislike humans. The animals are failing to make living like humans better than the humans do. Lifestyle of the pigs is far better than any of the other animals on the farm and it is seemingly unfair.Although the animal’s lifestyle is improving, it still seems that all the other animals are not being given the same treatment as the pigs have. The commandments are a model for all the animals to follow, but they are not really needed. On Animal Farm â€Å"the commandments are being written on the [tarred] wall with great white letters† (Orwell 24). The seven commandments be seen as a dynamic character because of their change in meaning o r what they are thought to mean, but are changing because of Squealer’s propaganda.With this the genre of Animal Farm is also the best example of what Stalin is doing in Russia. Although something may not be evenly in comparison there is a greater reason behind it. Boxer is the strongest and hardest working of all the animals, but he is also one that is least of value to all the pigs. Boxer’s maxims, â€Å"I will work harder(Orwell 125)† is a reminder to all the animals of what he and Animal Farm stands for. The motif of Boxer’s maxim is a perfect example for all the animals to follow.Also the animal’s only real motivation to work harder is that they all do not want Mr. Jones to return. Working hard for anything that has meaning pays off in the end. The success of all the animals has nothing to do with the pigs. â€Å"All animals are working like slaves, except the pigs (Orwell 59). † The windmill is a symbol of life to all the animals; it i s their only reason for living. Napoleon’s analogy of how the farm is now; to how it was when Mr. Jones was on the farm does not make sense. Success is on what is put into it; it is ll on how much effort is put forward. All in all someone or something, like the animals, is unjustly does not have the same equality as others do. The life of the pigs is made better because they make it, but this is not by the choice of the other animals. The pigs abuse their self obtainment of leadership and end up making life even harder for the other animals. All of the animals should be equal, and it has the assumption that they are, but they really are not. Equality is keen and should be properly in use all around the world.

Group Project 5 Tips for Writing

As a college student you will quite often get a task of preparing a group project in collaboration with one or several of your classmates. It may be an extremely taxing assignment, although not always due to the same reasons – especially if you don’t have a lot of experience of working in a group. In this article you will find several recommendations and tips that, hopefully, will make your work a little bit more agreeable. Plan Beforehand The main problem with group project is not, as you may think, difference of opinions and approaches, but a simple fact that you should work not alone, but together. The goal of the task is not so much to make you write something, but to teach you organization and teamwork. Although the Internet makes such collaboration much easier, you still have to gather together from time to time. Make a plan and make sure everybody follows it. Equal Distribution of Labor If you had any say in who you’ll have to work with, you probably already know strong and weak points of your collaborators. Try to organize yourselves so that each has roughly the same amount of work to do and does what he or she does best. However, sometimes (especially if it is your tutor who assigns people to groups) you will find your group weighed down by an entirely useless member. He can’t be trusted with anything, he either doesn’t do the task or somebody has to do it all over again afterwards. If it is possible, ask your tutor to get you rid of him. If not – don’t try to give him work for the sake of it, it is not worth it. Your main goal is to make a project, not to achieve justice. Define the Techniques You Are Going to Use in the Beginning Define how you are going to perform tasks. For example, what you will do if you cannot meet each other in person (e.g., use Skype conferences). How the editing process is to be organized. What to do if someone doesn’t do his share of work on time. How you are going to evaluate the work performed by each member. Unpleasant surprises will happen – you should be prepared. Report Regularly to Your Tutor You shouldn’t work in isolation from each other and from your tutor. He is not an enemy you should fool; treat him as a senior partner in your work. Report regularly to him – this way you will be able to track your own progress and, if necessary, receive assistance from the tutor, sometimes even when you don’t realize you need it. Be Dependable Teamwork asks for dependability, ability to correlate your schedules and courtesy. If you demand these things from collaborators, first demand them from yourself. Make sure that every member of the group keeps the entire project on his hard drive at all times – thus you will not lose the entire work even if one of you encounters technical problems.

Touch Someones Heart With Grateful Quotes

Wally Lambs I cried because I had no shoes. Then I met a man who had no feet, conveys a simple message: count your blessings.Often, you fail to appreciate simple pleasures and little blessings. You keep your eyes peeled for the big prize. A fancy car? Of course, you want it. An exotic vacation in the Far East? Sounds wonderful! A bigger house uptown? Sure. But what about the things you already have? Are you not grateful for that blessing called life?You can go on and on adding items to your wishlist; little realizing the precious seconds you waste by agonizing over unfulfilled dreams. When you see your wealthy neighbor show off his brand new Porsche, you may feel that yours is a life half lived. But instead of focusing on your object of envy, try focusing on the goodness of life. Material desires come and go, what remains with us is our ability to enjoy life and make the most of it. Ambition Is Not Bad, Greed Is It is not wrong to have ambition. By all means, keep your lofty goals in sight. Your ambition can be fueled by your passions, dreams, and desires. But dont fuel your ambition with greed. The hunger for success is not the same as the greed for fame. Greed is a selfish need to achieve ones objectives, even at the cost of others. Ambition propels you to innovate while living by the rules of fair play. Ambition is good for you; greed only makes you less grateful. Learn to Be Grateful As Joseph Addison rightly said, Gratitude is the best attitude. It takes more than humility to be grateful. Gratitude is ingrained into your psyche through social conditioning. Parents and teachers teach kids the magic words: Im sorry, please, thank you, excuse me, and youre welcome in preschool. As you mingle with others in social situations, you learn social etiquette that deems it necessary to express gratitude at appropriate occasions. Are you a Grateful Person? However, mere expressions of gratitude may not reveal whether a person is truly grateful. It could simply be lip service, or politeness, conveying nothing about the persons true feelings. If you are a grateful person, you can convey your appreciation in more than just words. Did your mom help you when you were sick? After you get well, celebrate your good health with your mother. Did your friend lend you the money you needed to set up shop? Repay the loan not only with interest but also with kindness. Did your friend help you get over a breakup? Hug your friend while saying, thanks, and promise to stick together in good and bad times. Make sure to live up to that promise. Express Thanks With Grateful Quotes Why stop at thank you, when you can say more? With grateful quotes, your words will tug at heartstrings. The listener will feel overpowered with the emotion contained in these quotes. Your generous words will win over friends.Richard CarlsonPeople who live the most fulfilling lives are the ones who are always rejoicing at what they have.Anthony RobbinsWhen you are grateful fear disappears and abundance appears.Marcel ProustLet us be grateful to people who make us happy; they are the charming gardeners who make our souls blossom.Nancy Leigh DeMossThe grateful heart that springs forth in joy is not acquired in a moment; it is the fruit of a thousand choices.SenecaNothing is more honorable than a grateful heart.Elizabeth CarterRemember that not to be happy is not to be grateful.Edgar Watson HoweNothing tires a man more than to be grateful all the time.Francois RochefoucauldWe seldom find people ungrateful so long as it is thought we can serve them.John MiltonA grateful mindBy owing owes not, but still pays, at onceIndebted and discharged.br/>Henry Ward BeecherA proud man is seldom a grateful man, for he never thinks he gets as much as he deserves.Robert SouthThe grateful person, being still the most severe exacter of himself, not only confesses but proclaims his debts.George HerbertThou who hast given so much to me, give me one more thing... a grateful heart!Steve MaraboliThose who have the ability to be grateful are the ones who have the ability to achieve greatness.Mary WrightWhen you say thank you it makes me feel like everything is good!Henry ClayCourtesies of a small and trivial character are the ones which strike deepest in the grateful and appreciating heart.Lionel HamptonGratitude is when memory is stored in the heart and not in the mind.Marcel ProustLet us be grateful to people who make us happy; they are the charming gardeners who make our souls blossom.Melody BeattieGratitude unlocks the fullness of life. It turns what we have into enough, and more.Chin ese ProverbWhen eating bamboo sprouts, remember the man who planted them.†Mary WrightThere is only one way to say thank you and thats just too straight up say, â€Å"Thank you.G. K. ChestertonI would maintain that thanks are the highest form of thought and that gratitude is happiness doubled by wonder.Sarah Ban BreathnachEvery time we remember to say â€Å"thank you†, we experience nothing less than heaven on earth.Albert SchweitzerTrain yourself never to put off the word or action for the expression of gratitude.Benjamin CrumpYour presence today spoke volumes. Thank you all for the support.Jill GriffinLearn to say thank you every time.