1) Proteins are biopolymers containing a large number of amino acids joined to each other by peptide linkages having three dimensional structures. The structure of proteins is a complex one which is divided into 4 parts. They are primary, secondary, teritiary and quaternary structures.
The simplest level of protein structure, primary structure, it is composed of various amino acids held together by peptide bonds. This structure is responsible for the function of a protein.
The next level of protein structure, secondary structure, refers to local folded structures that form within a polypeptide due to interactions between atoms of the backbone. The most common types of secondary structures are the α helix and the β pleated sheet. Both structures are held in shape by hydrogen bonds, which form between the carbonyl O of one amino acid and the amino H of another. In an α helix, C=O group of one amino acid is hydrogen bonded to the N-H group of another amino acid in the chain. In a β pleated sheet, two or more segments of a polypeptide chain line up next to each other, forming a sheet-like structure held together by hydrogen bonds.
The overall three-dimensional structure of a polypeptide is called its tertiary structure. It coils and folds in such a way that the hydrophobic side chains are held in the interior and the hydrophilic groups are held outside. This arrangement gives stability to the molecule.
Many proteins are made up of a single polypeptide chain and have only three levels of structure. However, some proteins are made up of multiple polypeptide chains, also known as subunits. The spatial arrangement of these subunits with respect to each other is known as quaternary structure.
2) Protein 3D structure is tertiary structure. The tertiary structure is maintained by hydrogen bonds, disulfide bonds, ionic bonds and hydrophobic interactions.
3) A protein family is a group of proteins that share a common evolutionary origin, reflected by their related functions and similarities in sequence or structure. Domains are distinct functional and structural units in a protein. Usually they are responsible for a particular function or interaction, contributing to the overall role of a protein.
1-3 thank you Define and describe protein 1 degree, 2 degree, 3 degree, 4 degree structure...
List and describe the two approaches to determining the tertiary structure of a protein. Experimental Determination Computational prediction There are three methods of computational structure prediction. Define each of the methods and describe when each method would be used. There are three types of helices formed by the secondary structure of protein. List three helices and rate how tightly coiled they are. Explain your reasoning. Choose any three of the twenty amino acids. Based on what you know about the...
please answer! 3) Protein structure and amino acid side chains a) Give examples of the types if attractive forces found between the side chains of the following amino acid residue pairs at pH 7.4 00 Leu and Phe (ii) Two Cys (ii) Asp and Thr (iv) Asp and Arg b) Of the 4 levels of protein structure, which ones are stabilized by interactions between amino acid side chains? c) Identify the two regular types of secondary structures and describe the...
1. What is protein structure? 2. Why is it important to know the primary structure? 3. What are the secondary structure elements in proteins? 4. How do we study protein structure? Mention at least 2 techniques. 5. What are some examples of basic amino acids and acidic amino acids?
After you eat a protein bar, define and describe the chemical reaction that links the individual amino acid together into new proteins that will be used by your individual cells
1. What are the levels of protein structure? 2. What is the role of myoglobin and describe the levels of protein structure that exists in myoglobin using PyMOL? 3. What types of forces exist to keep a protein in its native state? 4. What is denaturation? And describe some of the agents that cause denaturation.
Can you please describe the tertiary/quaternary structure of protein PDB#4M9X? I understand it is a complex of 4 chains (2 CED-4 chains & 2 CED-3 chains). The secondary structure of CED-4 includes alpha helices and beta sheets. I need to know how to describe the tertiary/quaternary structure of the protein complex. Thanks!
1. How can protein folding affect protein function? 2. How can amino acid sequence affect protein function? 3. How can an amino acid sequence (primary sequence) dictate 3D protein structure?
4. (a) Define the four levels of protein structure (primary, secondary, tertiary, and quaternary). (2 pt) (b) List four examples of types of interactions which give rise to tertiary structure. (2 pt) (c) What is protein denaturation, and list at least three ways this can be achieved. (2 pt)
6.) Provide short answers for the questions about protein structure below: a.) True or False, amino acid sequence defines the native structure of protein. b.) What is the main type of bonding responsible for stabilizing the secondary structure of proteins? c.) Briefly discuss the thermodynamics of protein folding into its native 3D structure. Is this process enthalpy driven or entropy driven? d.) Give an example of 2 major secondary structural motifs found in polypeptides. Do any of these motifs appear...
300 Full length protein Mutant protein 1 Mutant protein 2 75 300 1 250 Mutant protein 3 (fig69) 300 100 1 225 Mutant protein 4 Mutant protein 5 100 225 No protein Full length protein Mutant protein 1 Mutant protein 2 Mutant protein 3 Mutant protein 4 Mutant protein 5 (fig70) - In addition to cloning normal full length MYC, you make a series of mutant versions to identify the key functional domains of the protein. Based on similarity to...