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Exam (elaborations)

Biochemistry ACS Exam Questions and Answers 2024

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  • Biochemistry ACS
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  • Biochemistry ACS

structures and properties of amino acids Nonpolar, Aliphatic (Hydrophobic): Glycine (Gly, G) Alanine (Ala, A) Valine (Val, V) Leucine (Leu, L) Isoleucine (Ile, I) Proline (Pro, P) Aromatic (Hydrophobic): Phenylalanine (Phe, F) Tyrosine (Tyr, Y) Tryptophan (Trp, W) Polar, Uncharged (...

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  • August 29, 2024
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  • Biochemistry ACS
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Biochemistry ACS Exam Questions and
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BIOCHEM ACS
8/29/24

,Biochemistry ACS Exam

structures and properties of amino acids

Nonpolar, Aliphatic (Hydrophobic):
Glycine (Gly, G)
Alanine (Ala, A)
Valine (Val, V)
Leucine (Leu, L)
Isoleucine (Ile, I)
Proline (Pro, P)


Aromatic (Hydrophobic):
Phenylalanine (Phe, F)
Tyrosine (Tyr, Y)
Tryptophan (Trp, W)


Polar, Uncharged (Hydrophilic):
Serine (Ser, S)
Threonine (Thr, T)
Cysteine (Cys, C)
Methionine (Met, M)
Asparagine (Asn, N)
Glutamine (Gln, Q)


Positively Charged (Basic, Hydrophilic):
Lysine (Lys, K)
Arginine (Arg, R)
Histidine (His, H)


Negatively Charged (Acidic, Hydrophilic):



Biochemistry ACS Exam

, Biochemistry ACS Exam

Aspartic Acid (Asp, D)
Glutamic Acid (Glu, E)

protein structure

1. Primary Structure:
Definition: The primary structure of a protein is the linear sequence of amino acids that make
up the polypeptide chain.
Importance: The specific order of amino acids determines the protein's unique identity and
influences its folding and function.


2. Secondary Structure:
Definition: Secondary structure refers to the local folding patterns within a polypeptide chain.
The two most common secondary structures are alpha helices and beta sheets.
Alpha Helix:
A helical structure where the polypeptide chain coils like a spring.
Stabilized by hydrogen bonds between the carbonyl oxygen of one amino acid and the amide
hydrogen of an amino acid four residues away.
Beta Sheet:
A sheet-like structure where adjacent strands are connected by hydrogen bonds.
Can be parallel or antiparallel, depending on the direction of neighboring strands.


3. Tertiary Structure:
Definition: Tertiary structure refers to the overall three-dimensional arrangement of the entire
polypeptide chain, including its secondary structures.
Stabilizing Forces:
Tertiary structure is stabilized by various interactions, including hydrogen bonds, disulfide
bridges, hydrophobic interactions, and electrostatic attractions.
Folded Domains:
Proteins often consist of distinct folded domains, each with a specific function. Domains are
independently folded units within a protein.

Biochemistry ACS Exam

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