Brainscape's Knowledge GenomeTM


Top Flashcards (Certified)
All Flashcards

Medical Sciences - Biochemistry - Level 4 > Introduction: Biochemistry > Flashcards

Introduction: Biochemistry Flashcards

1
Q

What is entropy?

A

Going from order to disorder.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Entropy of Energy

A

Focus - Dispersed

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

Entropy of Information

A

High - Low

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

Entropy of Organisation

A

Complex - Simple

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

General Entropy

A

Life - Death

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Four main classes of biological molecule

A

Proteins Lipids Carbohydrates DNA (water)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Percentage of Biological Molecule Proteins

A

15-20%

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Percentage of Biological Molecule Lipids

A

10 -15%

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Percentage of Biological Molecule Carbohydrates

A

2%

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Percentage of Biological Molecule DNA / RNA

A

1%

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Percentage of Biological Molecule Water

A

50-65%

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Metabolism What is Catabolism?

A

Breakdown

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Metabolism What is Anabolism?

A

Synthesis (combination of separate elements to form a coherent whole - creating)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Metabolism must be tightly regulated by

A

Health Efficiency

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Metabolism is context dependent.

A

i.e. greater caloric intake for someone in the arctic to someone in the UK.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Proteins General

A

Large biomolecules Mr > 10,000 Da Most abundant organic compounds in healthy humans Formed of amino acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

Proteins General Roles

A

Cell structure Transport Catalysis Metabolic Regulation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

Amino Acids General

A

Amino acids are monomers, “building blocks” that bond to form peptide / protein polymers. 20 principal amino acids Same fundamental structure differentiated by side chains: asymmetric, “left handed” Essential / Non-essential

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

alpha-Amino acid structure

A

Chain of carboyx group. Alpha carbon with hydrogen and amino group. Side chain (residue; “R”) connected to alpha-carbon.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

Amino acids

Nonpolar

A

Glycine (Gly)

Alanine (Ala)

Valine (Val)

Leucine (Leu)

Isoleucine (Ile)

Methionine (Met)

Tryptophan (Trp)

Phenylalanine (Phe)

Proline (Pro)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

Amino acids

Polar

A

Serine (Ser)

Theronine (Thr)

Cysteine (Cys)

Tyrosine (Tyr)

Asparagine (Asn)

Glutamine (Gln)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

Amino Acids

Electrically Charged

Acidic

A

Aspartic Acid (Glu)

Glutamic Acid (Asp)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

Amino Acids

Electrically Charged

Basic

A

Lysine (Lys)

Arginine (Arg)

Histidine (His)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

Features of Amino Acids

Cysteine

A

Able to form Disulfide (S-S)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Features of Amino Acids Proline
Imide rather than Amide
26
Features of Amino Acids Buffering capabilities
Weak acid groups (COOH) Base groups (NH2)
27
Amino Acids Peptide
Amino acids linked by peptide bonds
28
Amino Acids Polypeptide
\>50 amino acids linked by peptide bonds
29
Amino Acids Proteins
Formed by one or more polypeptide chains
30
Residue meaning Table
Generic other atoms
31
Non-polar meaning
Electromag the same No significant +/- charge Hydrophobic
32
Polar meaning
Active groups Strong +/- charge Repel lipids
33
Acidic meaning
Releasing hydrogens
34
Basic
Accepting hydrogens
35
Primary structure Amino Acids Protein
Peptide bonds: link the alpha-amino group to the carbonyl group of thenext. Trans-arrangement: side chains of bonded as in opposite directions (except prolin, wich can be cis- or trans-) By convention, start at N-terminus and end at C-terminus No rotation around peptide bonds
36
Enzymes General function
Change shape to cause chemical reactions.
37
Secondary Structure
Local organisation polypeptide chains causedby folding. Primary structure determines how proteins fold. Folding assisted by chaperone proteins. Maintained by hydrogen bonds formed between amide and carboyl elements of peptide bonds.
38
Alpha helix Structure
3.6 a.a. residues per helix turn, 0.54nm pitch. Densely-packed, side chains on outside
39
Beta-pleated sheet
Parallel or anti-parallel rows of AAs linked by H-bonds. Pleated structure
40
Tertiary Structure
Geometric arrangement of a singly polypetide chain Contains multiple secondary structures Maintained by hydrophobic interactions, ionic bonds, disulfide bonds and hydrogen bonds,
41
Quaternary Structure What are oligomers?
Proteins made up of multiple polypetide subunits
42
Quaternary Structure homomers
All the same subunit
43
Quaternary Structure Heteromers
Different subunits
44
Quaternary Structure Subunits
Subunits helf together by non-covalent forces. Can undergo rapid conformational changes. These conformational changes enabe to facilitate protein functions.
45
Non-amino acid Protein Elements How are they further modified?
Attachment ofcarbohydrate, lipid, RNA groups. Atachment of small inorganic and organic molecules: metal ions, vitamins, methyl groups, phosphorylation, etc.
46
Non-amino acid Protein Elements How are they further modified? Cofactors
Usually metal ions or small organic molecules necessaru for protein activity
47
Summary of Protein Structure
Amino acids Peptide Bonds
48
Summary of Protein Structure Secondary structure
a-helix and B-pleated sheet
49
Summary of Protein Structure Tertiary Structure
Folded arrangement of polypeptide chain
50
Summary of Protein Structure Quaternary Structure
Subunit arrangement in oligomers
51
Types of Protein
Globular Proteins Fibrous Proteins Membrane Proteins
52
Types of Protein Globular proteins
Fold into roughly spherical shape. Usually water soluble. Enzymes, messengers, transporters. Usually insoluble.
53
Types of Protein Membrane Proteins
Embedded in the cell membrane, transmembrane or integral monotopic.
54
Globular Proteins Blood Proteins Albumins
\>50% of blood protein. Transports steriods, hormones, fatty acids, stabilises blood value.
55
Types of Protein Blood proteins Globulins
Various functions (e.g. inhibitors, immune system, etc.)
56
Globular proteins Haemoglobin General
4 subunits ("tetramer") in roughtly tetrahedral arrangement. Each subunit comprises multiple a-helices binding a heme group. Heme groups bind O2 / CO2 O2 bound in one heme induces conformation change to enhance binding at others.
57
Fibrous proteins Collagen General
Most abundant mammalian protein; \>20 types Trimer - 3 subunits wrapped in a helix, rich in glycine and proline. High strength - connective tissues (ligaments, tendons, skin), also bone, muscle, etc. Brittle bone disease is a mutation in collagen Type 1.
58
Fibrous Proteins Elastin General
Flexible - common in tissues requiring tension, stretching or deformation (lungs, arteries, bladder, skin, connective tissue) Covalently crosslinked polypeptides that are coiled at rest, but can stretch out Rich in non-polar aas, especially glycine, ananine, valine, proline. Smoking promotes elastin breakdown: emphysema, wrinkles.
59
Muscle proteins Actin & Myosin Actin
Globular monomers (G-actin) polymerise to fibrous, thin filament (F-actin)
60
Muscle proteins Actin & Myosin Myosin
Thick filament with globular "head" Conformational change when ATP is hydrolysed to ADP, pulling the actin filament.
61
Transmembrane Proteins
Transmembrane portion rich in hydrophoic alpha-helices. Often function by undergoing conformational changes Regulateactivity between extra- and intracellular Ion channels, transporters, receptors, enzymes.
62
Membrane proteins Ion channels
Proteins form pores that allow movement of ions and small molecules across the membrane. Gated ion channels undergo conformational changes to open or close the pore. Pentameric ion channel.
63
Cystic fibrosis transport conductance regulator
Gated channel Allows movement of Cl- Mutations prevent of impair Cl- movement leading to build-up of mucus
64
Membrane Proteins Cell adhesion Molecules
e.g. Integrins, Cadherins Bind cells to surroundings - other cells and extracellular matrix. Often linked to cystoskeleton.
65
Summary - Protein Function Structure
Globular - Spherical, usually soluble and free-floating Fibrous (usually involved in structural tissues) Membrane
66
Summary - Protein Function Function
Structural, Enzymes, Cell Transport, Carriers, Cell Signaling, Metabolic regulation

Medical Sciences - Biochemistry - Level 4 (5 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2025 Bold Learning Solutions. Terms and Conditions