Differences Between Science And Pseudoscience

The difference between a hypothesis and a scientific theory is that a hypothesis is a proposed description while a scientific theory is a proven description for something. The difference between a prediction and a hypothesis is that a prediction is a guess at what the results are going to be referring to the proposed hypothesis, while a hypothesis is a proposed explanation where the experiment will be based off of. A testable hypothesis would be useful in scientific experiments because it is testable, also a directional hypothesis would be good because it is based off of theories. A non-directional hypothesis would not be a good for investigations because they are based off on theories that have little or no grounds. In the cell theory, all

These proteins differ depending on their function in the cell, but often prevent misfolding of nascent protein, and assist in refolding of the misfolded proteins. Protein folding is dependent on the amino acid sequence within the polypeptide chain that is synthesized from the DNA strand in the ribosome.2 Upon release from the ribosome, the polypeptide chain undergoes a series of conformational changes based on the amino acid sequence to produce a functional protein structure. The assembled native protein is directed to the ER via vesicle

The structure of an enzyme as protein has a primary, secondary, tertiary, and sometimes quaternary structure. The primary structure of an enzyme, like any protein, is the order of its amino acids. The secondary structure involves alpha helices and beta pleated sheets. Alpha helices are a coil that is formed by hydrogen bonding between every fourth amino acid. Beta pleated sheets are formed by hydrogen bonding between two or more parts of the polypeptide chain that are side by side. The tertiary structure contains disulfide bridges, ionic bonds, hydrophobic interactions, and hydrogen bonds. Disulfide bridges are the result of two sulfhydryl groups interacting because the the folding of the protein. Ionic bonds can form between polar groups on amino acids. Hydrophobic interactions are the cluster of amino acids with nonpolar side chains that is commonly seen in proteins. Hydrogen bonds can also form. The quaternary structure of an enzyme is when multiple proteins are bonded together in one complex made of proteins subunits.

The tertiary structure of a protein molecule, or of a subunit of a protein molecule, is the arrangement of all its atoms in space, without regard to its relationship with neighboring molecules or subunits. Tertiary structure is simply the grouping of different separate secondary structures, such as multiple helices or multiple sheets or a combination of helices and sheets.

. The 3-D tertiary structure of polypeptide proteins globular and is the result of interactions that occur between R groups. Tertiary structure is a result of the bonds between sidechains of amino acids, the R groups. The structure and bonds involve alpha helices, beta pleated sheets, and also regions unique to each protein. Tertiary proteins are held together by four different types of forces; hydrogen bonds, hydrophobic interactions (including Van der Waals interactions), ionic bonding (electrostatic interactions), and disulfide bridges (strong covalent bonds). Hydrogen bonds occur within and between polypeptide chains and the aqueous environment. Hydrogen bonding forms between a highly electronegative oxygen atom or a nitrogen atom and a hydrogen atom attached to another oxygen atom or a nitrogen atom. This links the amino acid

Q41. There are several hydrogen bonds between the protein and the base pairs of the DNA such

The two main basic secondary structures are the alpha helix and the beta sheet. The alpha helix secondary structure of the protein coils because of the hydrogen bonds between the backbones of their amino acids. The backbone of the amino acid is the peptide bonds. So because of the hydrogen bonds forming between the amine nitrogens and the carbonyl oxygens in different amino acids the protein has become a helix shape.

Tertiary Folding includes hydrogen bonds as well as disulfide bridges. Hydrogen bonds can form between side-chain groups. As with the disulfide bridges, these hydrogen bonds bring together two parts of a chain that are a distance away from each other in terms of sequence. These bonds are important because they help to form and stabilize the overall 3D structure of the protein.

These protein macromolecules consist of a sequence of amino acids and are 3D because of the quaternary structure. Primary structure, like all proteins or polypeptides, includes a sequence of particular amino acids, which is established by certain genes in DNA, linked together by peptide bonds in the linear chain. The second structure is due to Hydrogen bonds between amino groups (NH2) and carboxyl (COOH) group. Consequently, the chain folds upon itself and forms α-helix or β-sheet. Therefore, a protein can fold even further, getting itself a three-dimensional structure.

An enzyme is a ‘protein (or in few cases RNAs) that are highly specific for the reactions they catalyze’1 as it is a protein it would consist of the primary, secondary, tertiary, and quaternary structure. The primary structure has a sequence of amino acids in a polypeptide chains, the secondary structure consists of polypeptide chains that are either twisted or coiled – the two common structures are α-helices and ß-pleats. Weak hydrogen bonds hold coils in place and many are formed so it provides overall stability2. The tertiary structure would be the secondary structure being coiled even further being held together by weak hydrogen bonds, disulphide bridges and ionic bonds. The quaternary structure is when there is two or more polypeptide

Bettelheim, Brown, Campbell and Farrell assert that polypeptide chains do not extend in straight lines but rather they fold in various ways and give rise to a large number of three-dimensional structures (594). This folding or conformation of amino acids in the localized regions of the polypeptide chains defines the secondary structure of proteins. The main force responsible for the secondary structure is the non-covalent

3. The structure of a protein such as hemoglobin is very similar to an enzyme. The primary structure is the amino acid sequence. The secondary structure is the bonding of primary structures with the use of hydrogen. Tertiary structure is the bonding of the previous stage by covalent bonds. The final Quarternary structure involves more than one amino acid sequence. When a protein such as hemoglobin is heated, its bonds will be broken, causing a delay on the speed in which it is able to carry oxygen.

2014). Ultimately, a protein can take on the tertiary structure which is a combination of all the secondary structures (Alberts, B. 2014). Furthermore, most proteins take on the quaternary structure which consist of two or more polypeptide chains that form a protein complex of a honomer or heteromer (Alberts, B. 2014).

Karl Popper expands this idea by saying that what makes something scientific is the concept of it being falsifiable, rather than a method that results in absolute truth (Jogalekar, 2014). This means that in order for a theory to be scientific it has to have the possibility of being tested to be false or incorrect. According to Popper, this is also

Hypothesis: A hypothesis is a Testable prediction about the relationship between two or more variables. Hypothesis predicts what the psychologist expects to see during