B1.2.1– generalized structure of an amino acid

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23 Terms

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can essential amino acids be synthesized?

No. it must be obtained from food. Vegan diets require attention to ensure essential amino acids are consumed. Non-essential amino acids can be made from other amino acids.

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How is a peptide bond formed

a ribosome condenses two amino acids into a dipeptide

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is DNA code variable or narrow?

highly variable!

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Does protein length have a limit? What is the shortest and longest polypeptide?

No. it can be any length.

Shortest: 11 AAs long

Longest: Titin, 35,000 AAs long.

there are infinite combos!

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denaturation

changing of a proteins 3D shape. it is considered irreversible.

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Effect of temperature on protein structure

-heat will denature a protein

-cold does not!

-Most animal proteins are stable at body temperature. Plant proteins are stable at air temps.

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effect of pH on protein structure

-pH denatures proteins

-any pH outside of optimal range will cause loss of 3D structure

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Primary structure of amino acid

Sequence of amino acids as a result of gene sequence.

R-group will matter later

<p>Sequence of amino acids as a result of gene sequence.</p><p>R-group will matter later</p>
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secondary structure of amino acid

Amino and Carbonyl groups will interact to form Hydrogen bonds.

a-helix will form a spiral structure

Beta-pleated sheets form.

<p>Amino and Carbonyl groups will interact to form Hydrogen bonds.</p><p>a-helix will form a spiral structure</p><p>Beta-pleated sheets form.</p>
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Tertiary Structure

R-group matters here!

3D folding due to R-group interactions (e.g., hydrophobic, ionic, disulfide)

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tertiary and primary structure relationship

if primary structure changes, tertiary could change.

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R groups

each of the 20 amino acids have unique R-groups

R-groups can be positive or negatively charged, acidic, basic polar, or non-polar

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Cysteine

a sulfur containing amino acid. Disulfide bridges are critical to lots of tertiary structure

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How do proteins work in watery enviornemnts?

in globular proteins, hydrophobic amino acids are clustered in the middle. keeps it working.

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Quaternary structure

Multiple polypeptide chains joined to form one functional protein

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conjugated proteins quaternarny

have another molecule in their quaternary structure

Hemoglobin has iron!

Glycoproteins hhave carbohydrates attatched!

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non-conjugated proteins quaternary

Purely protein in their quat structure

Insulin!

collagen!

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Collagen

long, fibrous protein that formed fibers and can run thru tissue. It makes your skin tight and bones strong

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Actin and Myosin

long, fibrous proteins that form cellular cytoskeleton and muscle fibers!

Actin is pulled by myosin to contract a muscle!

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Enzymes

globular proteins w a specific 3D shape that binds to other molecules at a specific active site.

They can change shape to catalyze reactions

<p>globular proteins w a specific 3D shape that binds to other molecules at a specific active site.</p><p>They can change shape to catalyze reactions</p>
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insulin

globular protein that fits into a receptor that is coupled w/ a glucose channel in cell membranes.

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How does insulin work?

WHen insulin binds, the channel opens, allowing glucose to leave blood and enter cells

<p>WHen insulin binds, the channel opens, allowing glucose to leave blood and enter cells</p>
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cyro-electron microscopy

allowed us to visualize proteins for first time