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King's Year 1 BDS: Body Systems · Meedu

Course
Dentistry

King's Year 1 BDS: Body Systems

Protein Structure & Function

Movement of Ions & Molecules

Electrochemical Equilibria

Cell Signalling 1

Cell Signalling 2

Organisation of the Nervous System

Electrical Properties of Cells

Muscle Contraction

Communication Between Excitable Cells

Introduction to Pharmacology

Pharmacological Perspective of the Autonomic Nervous System

Interruption of Neurotransmission in Dental Treatments

Metabolism Overview

Glucose & Glycogen Metabolism

TCA Cycle & Oxidative Phosphorylation

Energy Release From Fat

Amino Acid & Protein Metabolism

Fat Storage & Transport

Integration of Metabolism

Cell Nucleus, Chromosomes & Cell Division

DNA: Structure & Replication

Gene Expression: Transcription & Translation

Control of Gene Expression

Chromosomal Abnormalities, Single Gene & Multifactorial Disorders

Applying Genomic Technologies in the Clinic

Genetics Scenario Review

Biochemistry Tutorial 4: Genetics

King's Year 1 BDS: Body Systems

Year 1 Body Systems module at King's College London Dental Institute. Foundational biomedical science covering macromolecules & cell biology, nervous system & pharmacology, metabolism, and genetics — spanning BD1F-MAC, BD1F-NVS, BD1F-MET and BD1F-GEN lecture strands.

A

B

C

D

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CategoryDentistry

Duration9 Months

/24

A peptide chain folds into a stable α-helix. Which consequence directly arises from the specific hydrogen-bonding registry observed in this secondary structure?

Select the correct answer

A. Each residue's carbonyl group is hydrogen-bonded to the amide of the immediately adjacent residue, creating a highly compact turn1

B. Hydrogen bonds form between residues n and n+3, allowing three full residues to complete each helical turn2

C. The side chains of residues separated by four positions in sequence are held in close proximity, enabling direct side-chain hydrogen bonding within the helix core3

D. Hydrogen bonds form exclusively between antiparallel strands, orienting all carbonyl groups perpendicular to the helix axis4

E. Residues spaced four apart in the primary sequence are brought into hydrogen-bonding proximity, meaning every 3. 6 residues complete one helical turn with all backbone carbonyls aligned roughly parallel to the helix axis5

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