NUTR 200 Lecture Notes - Lecture 11: Sickle-Cell Disease, Enterocyte, Collagen
31 May 2018
School
Department
Course
Professor
NUTR 200 Nutrition for Today 4/18/2018
MJ Gunnarson, MS, RD 1
Protein and amino acids 1
Reading
p 163-175
Chapter 8 – Introduction, Recommendations for Protein Intake, Structure of Protein, Protein
Synthesis, Digestion and Asorption…, Varied Funtions..., Protein Turnover and Nitrogen Balane
Objectives for today:
• Explain why essential amino acids are essential.
• Identify the two main steps in protein synthesis.
• Define nutrigenomics.
• Describe how proteins are digested and absorbed by the body.
• List some different functions of proteins in the body.
Protein Facts
Contain C, H, O and nitrogen
Regulate and maintain body functions
Supply energy (4 kcal/g)
Amino Acids (building blocks of proteins): contain a central carbon atom, an amino group that
contains an atom of nitrogen, an acid group, a hydrogen atom, and a side chain (unique)
• Lined together by peptide bonds
• Dipeptides have 2 amino acids
• Tripeptides have 3 amino acids
• Polypeptides have many amino acids
Bound together using peptide bonds: form when a COOH group and amino group attach each
other
Essential
Cannot be produced by our bodies
find more resources at oneclass.com
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NUTR 200 Nutrition for Today 4/18/2018
MJ Gunnarson, MS, RD 2
Must be obtained from food
Non-essential
Protein synthesis
Conditionally essential:
Phenylalanine-- tyrosine
PKU (phenylketonuria): enzyme phenylalanine hydroxylase not functional
Transcription
• Making mRNA from DNA
• Convert info (DNA) into readable instructions (mRNA)
Translation
• Making protein from mRNA
• Convert readable instructions (mRNA) into protein product
Folding and function
- Shape determines the function of the protein
-after translation, amino acid chains fold into a particular shape
Primary structure
Side chains of amino acids in primary structure lead to folding of the protein
Examples –
-structural proteins like collagen
---consist primarily of long straight polypeptides
-hemoglobin
---has polypeptides folded into a spherical structure adapted to hold oxygen atoms
---changes in shape: sickle cell anemia
-enzymes
find more resources at oneclass.com
find more resources at oneclass.com
Document Summary
Chapter 8 introduction, recommendations for protein intake, structure of protein, protein. Synthesis, digestion and a(cid:271)sorption , varied fun(cid:272)tions, protein turnover and nitrogen balan(cid:272)e. Amino acids (building blocks of proteins): contain a central carbon atom, an amino group that contains an atom of nitrogen, an acid group, a hydrogen atom, and a side chain (unique) Lined together by peptide bonds: dipeptides have 2 amino acids, tripeptides have 3 amino acids, polypeptides have many amino acids. Bound together using peptide bonds: form when a cooh group and amino group attach each other. Transcription: making mrna from dna, convert info (dna) into readable instructions (mrna) Translation: making protein from mrna, convert readable instructions (mrna) into protein product. Shape determines the function of the protein. After translation, amino acid chains fold into a particular shape. Side chains of amino acids in primary structure lead to folding of the protein. --has polypeptides folded into a spherical structure adapted to hold oxygen atoms.
