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Research draft

transmembrane protein

vr.tr.transmembrane-protein · PHY.MAT

Let an agent explain transmembrane proteins and their structure, relay classes, functions and study methods from biochemistry references, describe membrane-active toxins and peptides at the level of published biology, and distinguish transmembrane proteins from peripheral membrane proteins, lipid-anchored proteins and secreted proteins.

Thing Registry Physical world and living systems

Research draft, second pass

A second pass drafted this model: the structure a model of this thing needs, and what is known about it in the world. The line under this one says how the second half was obtained - researched against sources, or recalled without web access, in which case nothing here was read anywhere and every claim is a lead to verify. Unreviewed either way.

written by Claude from model knowledge without web access - no source was read, every claim is a lead to verify

Researched by: Claude

Purpose and description

Let an agent explain transmembrane proteins and their structure, relay classes, functions and study methods from biochemistry references, describe membrane-active toxins and peptides at the level of published biology, and distinguish transmembrane proteins from peripheral membrane proteins, lipid-anchored proteins and secreted proteins.

A protein that spans the whole cell membrane, with domains on both sides, forming channels, transporters, receptors and enzymes essential to cell function, and including membrane-inserting proteins listed in the registry aliases such as pore-forming toxins, snake three-finger toxins that bind receptors, defensins of insects, fungi and plants, and antimicrobial peptides such as tachyplesin and oxyopinin that disrupt membranes; the model covers structure and biology without any guidance on toxin production or use.

What it is for: Not applicable; a protein class.

It can be explain structure and classes; relay functions and methods; describe membrane-active molecules; distinguish related proteins.

Distinguishing features

Spans the bilayer

Alpha-helical or beta-barrel

Channels and receptors

Toxin and peptide relatives

What it looks like

Not a visible object; proteins spanning the lipid bilayer.

Physical character

share of human genes: about 25-30 percent - encode membrane proteins

main folds: alpha-helical bundles and beta-barrels list

drug targets: over half of drugs target membrane proteins note

How it is recognised

Protein spanning the membrane

Channels, transporters, receptors; pore-forming toxins, three-finger toxins, defensins, tachyplesin, oxyopinin

Peripheral proteins attach to the surface; lipid-anchored proteins are tethered; secreted proteins leave the cell

Related models

is a kind of - in registry terms

integral membrane protein

is embedded in - the lipid bilayer

cell membrane

is contrasted with - attached to the surface

peripheral membrane protein

is exemplified by - a major class

ion channel

In practice

Families and kinds

ion channels and transporters

G protein-coupled and other receptors

membrane enzymes

beta-barrel outer membrane proteins

pore-forming toxins and membrane-active peptides such as defensins, tachyplesin and oxyopinin

three-finger toxins that target membrane receptors

Identifiers

GO GO:0016021 membrane, integral component

Standards and regulation

No regulation of the protein class; biosafety rules apply to toxin research

Failure modes and hazards

Agents providing toxin production or use guidance

Confusing transmembrane with peripheral proteins

Registry aliases naming toxins and peptides as if kinds of transmembrane protein

Also called

pore-forming toxinsnake three-finger toxininsect/fungal defensinplant defensinTachyplesinOxyopininMembrane attack complex component/perforin/complement C9prion protein familyVacuolating cytotoxinPro-islet amyloid polypeptideHemolytic lectin CEL-III, C-terminal domain superfamilygasderminPentraxinMastoparan familyPleurocidinMoricin familyAerolysinAurein antibiotic peptide familycecropinEpsilon toxinLipid binding protein BPI/LBPBacteriocin, lactococcin 972PleurotolysinClostridial Cytotoxin familydermaseptinsESAT-6-like superfamilyArenicinbeta defensincholesterol-dependent cytolysinCytolethal distending toxinHaemolysin Eyeast killer toxin familydiphtheria toxin familyRTX toxinCytohemolysinMelittin familyAmoebapore familyType III-Target Cell PoreEquinatoxintripartite haemolysin BL

+279

Where this came from

wikidata · CC0 1.0

Drafted structure

Bundle to layer to finding to question, as the second pass will find it: 4 bundles · 8 layers · 8 findings · 16 questions.

Understand What a transmembrane protein is.

Science.

Definition

Definition and structure.

Definition

Definition.

  1. What is a transmembrane protein, and how does it differ from peripheral, lipid-anchored and secreted proteins? definition
  2. Is the question about structure, function, a class, or toxin use, which the model does not assist? boundary

Classes

Classes.

Classes

Classes.

  1. What are channels, transporters, receptors, membrane enzymes and beta-barrel proteins? definition
  2. Which entry fits the specific class? action
Biology Biology.

Science.

Function

Function.

Function

Function.

  1. How do transmembrane proteins transport ions and molecules, transmit signals and catalyse reactions? provenance
  2. Which references are standard? provenance

Folding

Insertion and folding.

Folding

Folding.

  1. How are transmembrane proteins inserted and folded in the membrane? provenance
  2. Which sources are cited? provenance
Active Membrane-active molecules.

Science.

Toxins

Toxins.

Toxins

Toxins.

  1. What are pore-forming toxins and three-finger toxins, and how do they act, at the level of published biology? provenance
  2. Is the presentation limited to biology without production or use detail? boundary

Peptides

Antimicrobial peptides.

Peptides

Peptides.

  1. What are defensins, tachyplesin and oxyopinin, and why are they studied for antimicrobials? provenance
  2. Which entry fits antimicrobial peptide? action
Context Methods and medicine.

Context.

Methods

Study methods.

Methods

Methods.

  1. How are membrane proteins studied by cryo-EM, crystallography and prediction? provenance
  2. Which entry fits membrane protein structure? action

Medicine

Drug targets.

Medicine

Medicine.

  1. Why are membrane proteins major drug targets, and what diseases involve them? provenance
  2. Which entry fits G protein-coupled receptor? action

What the second pass must settle

  • Should pore-forming toxin and defensin be separate primary entries?
  • How should biochemistry references be linked?
  • The registry entry has merged aliases naming toxins and antimicrobial peptides; should they be split off?