CADD QUIZ

An illustration of computer-aided drug design with molecular structures and computer graphics.

Test Your Knowledge on Computer-Aided Drug Design

Welcome to the CADD Quiz! This quiz is designed to assess your understanding of various concepts related to Computer-Aided Drug Design. Whether you are a student, researcher, or simply curious about the field, this quiz will challenge your knowledge and reinforce your learning.

Key features of the quiz:

11 carefully crafted multiple-choice questions
Covers essential topics in drug design and protein structure
Fun and engaging way to test your knowledge

11 Questions3 MinutesCreated by ExploringMolecule24

A drug discovery process that allows automated testing of large numbers of chemical and/or biological compounds for a specific biological target

High-throughput Screening

Virtual Drug Screening

Drug Lead Optimization

______________________ is a term that comprehensively represents computational analysis of a DNA, RNA or peptide sequence, to extract knowledge about its properties, biological function, structure and evolution.

Data Mining

Sequence Analysis

Sequence Alignment

Biological Sequence

A procedure that generates a previously unknown protein structure by “fitting” its sequence (target) into a known structure (template), given a certain level of sequence between target and template.

Protein Modeling

Homology Modeling

Which statements is FALSE about Drug Bioavailability?

Bioavailability refers to the extent and rate at which the active moiety (drug or metabolite) enters systemic circulation, thereby accessing the site of action.

Bioavailability of a drug is largely determined by the properties of the dosage form, which depend partly on its design and manufacture

Bioavailability is “the capacity of a specific molecular entity to achieve a defined biological effect” on a target.

Which statements is FALSE?

The four levels of protein structure are primary, secondary, tertiary, and quaternary.

Secondary structure is local interactions between stretches of a polypeptide chain and includes α-helix and β-pleated sheet structures.

Tertiary structure is the overall the three-dimension folding driven largely by interactions between planar group.

What do alpha helices and beta sheets have in common?

Both structures allow formation of the maximum possible number of peptide bonds.

Both structures allow formation of the maximum possible number of covalent bonds.

Not stable.

Both structures allow formation of the maximum possible number of hydrogen bonds

Protein tertiary structure can be divided into four main classes based on the secondary structural content of the domain. Which following statement is FALSE?

All-α domains have a domain core built exclusively from α-helices. This class is dominated by small folds, many of which form a simple bundle with helices running up and down.

All-β domains have a core composed of antiparallel β-sheets, usually two sheets packed against each other. Various patterns can be identified in the arrangement of the strands, often giving rise to the identification of recurring motifs, for example the Greek key motif.

α+β domains are a mixture of all-α and all-β motifs. Classification of proteins into this class is difficult because of overlaps to the other three classes and therefore is not used in the CATH domain database

α/β domains are made from a combination of α-β-α motifs that predominantly form a parallel β-sheet surrounded by amphipathic α-helices. The secondary structures are arranged in layers or barrels.

CADD QUIZ

Test Your Knowledge on Computer-Aided Drug Design

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