IB Biology HL - Proteins (B1.2) Vocabulary

0.0(0)
studied byStudied by 0 people
learnLearn
examPractice Test
spaced repetitionSpaced Repetition
heart puzzleMatch
flashcardsFlashcards
Card Sorting

1/23

flashcard set

Earn XP

Description and Tags

Flashcards for IB Biology HL - Proteins (B1.2)

Study Analytics
Name
Mastery
Learn
Test
Matching
Spaced

No study sessions yet.

24 Terms

1
New cards

Amino Acid

Monomer of proteins; there are 20 different amino acids in nature.

2
New cards

Amine Group

Basic functional group found in amino acids (-NH₂).

3
New cards

Carboxyl Group

Acidic functional group found in amino acids (-COOH).

4
New cards

Alpha Carbon

Central carbon (Cα) in an amino acid, bonded to the amine, carboxyl, hydrogen, and R group.

5
New cards

R Group (Side Chain)

Determines the properties and identity of each amino acid.

6
New cards

Peptide Bond

Covalent bond formed during a condensation reaction between amino acids.

7
New cards

Dipeptide

Two amino acids linked together via a peptide bond.

8
New cards

Oligopeptide

A chain of 3-20 amino acids linked by peptide bonds.

9
New cards

Polypeptide

A chain of more than 20 amino acids linked by peptide bonds.

10
New cards

Hydrophilic Amino Acids

Amino acids generally found on the exterior of proteins, interacting with water molecules.

11
New cards

Hydrophobic Amino Acids

Amino acids generally found in the interior of proteins, avoiding water molecules.

12
New cards

Primary Structure

The amino acid sequence of a polypeptide chain.

13
New cards

Secondary Structure

The pleating and coiling of proteins due to hydrogen bonding (alpha-helix and beta-pleated sheet).

14
New cards

Tertiary Structure

The 3D shape of a protein held together by hydrogen bonds, ionic bonds, disulfide bonds, and hydrophobic interactions among R-groups.

15
New cards

Quaternary Structure

The arrangement of two or more polypeptide subunits or a polypeptide conjugated with a prosthetic group.

16
New cards

Disulfide Bonds

Covalent bonds formed between cysteine amino acids, contributing to the tertiary structure of proteins.

17
New cards

Globular Proteins

Soluble, compact, and functional proteins (e.g., insulin).

18
New cards

Fibrous Proteins

Insoluble, long, and strong proteins serving structural roles (e.g., collagen).

19
New cards

Denaturation

The process where a protein loses its shape due to changes in pH or temperature, leading to loss of function.

20
New cards

Nonessential Amino Acids

Amino acids that animals can synthesize under most conditions (11).

21
New cards

Essential Amino Acids

Amino acids that animals cannot synthesize and must obtain through diet (9).

22
New cards

Complete Protein

A protein source that contains all 9 essential amino acids.

23
New cards

Incomplete Protein

A protein source that lacks one or more of the essential amino acids.

24
New cards

Cryo-EM

Cryogenic electron microscopy, a modern imaging technology allowing visualization of single-protein molecules at near-atomic detail.