How are proteins given a functional characterization if they have not been experimentally studied? The location of charges on a protein will accurately predict function Conserved stretches of amino acids can fold into stable structures independently of the rest of the protein and perform distinct functions

Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:Elaine N. Marieb, Katja N. Hoehn
Chapter1: The Human Body: An Orientation
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**How are proteins given a functional characterization if they have not been experimentally studied?**

- ○ The location of charges on a protein will accurately predict function
- ○ Conserved stretches of amino acids can fold into stable structures independently of the rest of the protein and perform distinct functions
- ○ Nonpolar amino acids are buried on the inside of the protein
- ○ Both polar amino acids are oriented outward and nonpolar amino acids are buried on the inside of the protein
- ○ Polar amino acids are oriented outward where they interact with water
Transcribed Image Text:**How are proteins given a functional characterization if they have not been experimentally studied?** - ○ The location of charges on a protein will accurately predict function - ○ Conserved stretches of amino acids can fold into stable structures independently of the rest of the protein and perform distinct functions - ○ Nonpolar amino acids are buried on the inside of the protein - ○ Both polar amino acids are oriented outward and nonpolar amino acids are buried on the inside of the protein - ○ Polar amino acids are oriented outward where they interact with water
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Proteins are macromolecules made up of a long-chain of amino acid units. They are required by the body to function effectively. Proteins in the form of enzymes regulate the body to perform many important biochemical processes and chemical reactions. in nature, there are 20 amino acids found in the human body. There is four well-known structure of the protein and they are primary, secondary tertiary and quarternary structure.

Protein structure is formed by condensation of amino aicds to give a first primary structure and they further fold to give a three-dimensional protein. With the help of forces such as covalent force, weak Vanderwall force, and hydrogen bond a specific conformational folding of the protein takes place that gives a protein definite biological function.

 

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