Aminoacids and Proteins Flashcards Preview

HFF - Exam I > Aminoacids and Proteins > Flashcards

Flashcards in Aminoacids and Proteins Deck (19):

What is a Ketogenic amino acid?

Ketogenic amino acids are those amino acids that are converted to acetyl CoA or Acetoacetate which are precursors to ketone bodies


What are Glucogenic amino acids?

Are those amino acids which are converted to precursors for glucose synthesis like alpha-ketoglutarate, succinyl CoA, Fumarate


What is the general structure of all amino acids except for Glycine

The alpha carbon is a chiral center.


Name all amino acids in the Non-polar, aliphatic group

1. Glycine 2. Alanine 3. Proline 4. Valine 5. Leucine 6. Isoleucine 7. Methionine

A image thumb

Name all amino acids in the Aromatic group

1. Phenylalanine 2. Tyrosine 3. Tryptophan

A image thumb

Name all amino acids in the Polar, uncharged group

1. Serine 2. Threonine 3. Cysteine 4. Asparagine 5. Glutamine

A image thumb

Name all amino acids in the Positively charged group

1. Lystine 2. Histidine 3. Arginine

A image thumb

Name all amino acids in the Negatively charged group

1. Asparate 2. Glutamate

A image thumb

Stereoisomerism in Alpha aminoacids

A image thumb

The amino acids are all chiral except for ______?



All naturally occurring proteins from all living organisms conist of (L or D) Amino acids?

L amino acids


What is a zwitterion?

A zwitterion is neutral molocule with a positive AND a negative electrial charge, though multiple positive and negative charges can be present

A image thumb

Define a Protein

Proteins are polymers built from amino acids joined by PEPTIDE BONDS


Explain the different structures of Proteins (ie) Primary, secondary ect....

A image thumb

Give an example of how a single amino acid can alter the function of a protein

Normal red blood cells to sickle cell blood cells.... just one amino acid is changed and completely changes the function of the cell.


Define Proteostasis

Refers to the process by which cells control the abundance and folding of the proteome, and consists of a highly interconnected network that integrates the regulation of gene expression, signaling pathways, molecular chaperones and protein degredation systems. 


What CANT a protein lose even when it is denatured?

A protein can never lose its PRIMARY structure even when denatured. When a protein is in its Unfolded state, it becomes inactive. 


What famous disease is related to Collagen

Scurvy (Vitamin C defiency)

Osteogenesis Imperfecta: a person has too little type I collagen or a poor quality of type I collagen due to a mutation in one of the type I collagen genes


Explain the steps of Collagen Synthesis

A image thumb