What is the relationship between a protein's structure and its ability to function? | Socratic
The function of a protein is determined by its shape. The shape changes in pH (alters electrostatic interactions between charged amino acids); changes in salt. Learn how their functions are based on their three-dimensional structures, which Figure 1: The relationship between amino acid side chains and protein. The holy grail of computational biology is the elucidation, at a molecular, cellular and biological level, of function. As we tried to illustrate here, several routes are.
The membrane-spanning regions of membrane proteins are typically alpha helices, made of hydrophobic amino acids. These hydrophobic regions interact favorably with the hydrophobic lipids in the membrane, forming stable membrane structures.
Protein Structure and Function - Biochemistry - NCBI Bookshelf
Hemoglobin is a soluble protein - found in the cytoplasm of red blood cells as single molecules - which bind oxygen and carry it to the tissues. In sickle cell anemia, a mutation in the beta-globin protein of the red blood cell increases its hydrophobicity and causes the mutant protein molecules to stick to each other, avoiding the aqueous environment.
Chains of hemoglobin change the shape of the red blood cell from round to a sickle shape, which causes the cells to collect in narrow blood vessels. Active site The folding of a protein allows for interactions between amino acids that may be distant from each other in the primary sequence of the protein.
- What is the relationship between a protein's structure and its ability to function?
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Remarkably, proteins spontaneously fold up into three-dimensional structures that are determined by the sequence of amino acids in the protein polymer. Thus, proteins are the embodiment of the transition from the one-dimensional world of sequences to the three-dimensional world of molecules capable of diverse activities. Proteins contain a wide range of functional groups. These functional groups include alcohols, thiols, thioethers, carboxylic acids, carboxamides, and a variety of basic groups.
The Rules of Protein Structure
When combined in various sequences, this array of functional groups accounts for the broad spectrum of protein function. For instance, the chemical reactivity associated with these groups is essential to the function of enzymes, the proteins that catalyze specific chemical reactions in biological systems see Chapters 8— Proteins can interact with one another and with other biological macromolecules to form complex assemblies.
As mentioned above, high temperatures can denature proteins, and when a cell is exposed to high temperatures, several types of molecular chaperones swing into action. For this reason, these chaperones are also called heat-shock proteins HSPs. Not only do molecular chaperones assist in the folding of newly-synthesized proteins, but some of them can also unfold aggregated proteins and then refold the protein properly.
Protein aggregation is the cause of disorders such as Alzheimer's diseaseHuntington's diseaseand prion diseases e.The relationship between structure and function of proteins
Perhaps some day ways will be found to treat these diseases by increasing the efficiency of disaggregating chaperones. Despite the importance of chaperones, the rule still holds: And the sequence of amino acids in every protein is dictated by the sequence of nucleotides in the gene encoding that protein.
Rules of Protein Structure
So the function of each of the thousands of proteins in an organism is specified by one or more genes. There are some cases where a protein can exist in more than one conformation; that is, a given primary structure can give rise to two or more different tertiary structures.
Link to an example.