Help & Documentation

Everything you need to know about visualizing and analyzing peptide structures

🚀 Quick Start Guide

Get started with PepDraw in just a few simple steps:

1
Enter Your Sequence

Type directly into the sequence field or click amino acid buttons using single-letter codes (A, C, D, E, F, G, H, I, K, L, M, N, P, Q, R, S, T, V, W, Y).

2
Adjust pH (Optional)

Use the pH slider to see how ionizable amino acids change their protonation states at different pH values.

3
View Structure & Properties

Watch the chemical structure render in real-time along with calculated properties like mass, pI, charge, and hydrophobicity.

4
Export Your Visualization

Download free images in PNG or JPG format. Pro feature coming soon: SVG and PDF format for use in scientific publications, presentations, or educational materials.

Try PepDraw Now →

About PepDraw

PepDraw is a powerful yet user-friendly tool designed to facilitate the study of peptide chemical structures and properties. It allows researchers, students, and educators to:

💡 Educational Excellence

PepDraw is especially useful for teaching students about amino acid structure and properties. The real-time visualization helps bridge the gap between sequence and structure.

Sequence Entry

Method 1: Direct Typing

Type your peptide sequence directly into the sequence entry field using standard single-letter amino acid codes. PepDraw automatically recognizes and processes the 20 standard amino acids.

Example: ACDEFGHIKLMNPQRSTVWY

Method 2: Amino Acid Keypad

Click the buttons in the amino acid palette to build your sequence one residue at a time. This method is great for beginners or when teaching amino acid structures.

✓ Valid Characters

PepDraw reads only the 20 standard amino acid codes: A, C, D, E, F, G, H, I, K, L, M, N, P, Q, R, S, T, V, W, Y. Any other characters will be ignored.

Standard Amino Acids

Code Amino Acid Properties
AAlanineHydrophobic, small
CCysteinePolar, can form disulfides
DAspartic acidAcidic, negatively charged
EGlutamic acidAcidic, negatively charged
FPhenylalanineAromatic, hydrophobic
GGlycineSmallest, flexible
HHistidineBasic, aromatic, pH-sensitive
IIsoleucineHydrophobic, branched
KLysineBasic, positively charged
LLeucineHydrophobic, branched
MMethionineHydrophobic, contains sulfur
NAsparaginePolar, uncharged
PProlineCyclic, creates kinks
QGlutaminePolar, uncharged
RArginineBasic, positively charged
SSerinePolar, small
TThreoninePolar, can be phosphorylated
VValineHydrophobic, branched
WTryptophanAromatic, hydrophobic, largest
YTyrosineAromatic, polar

Peptide Properties Explained

PepDraw automatically calculates comprehensive peptide properties as you enter your sequence. All calculations update in real-time.

Sequence
Your peptide sequence displayed in standard single-letter code format, exactly as analyzed by PepDraw.
Sequence Length
The number of valid amino acid residues in your peptide. This excludes any terminal modifications.
Molecular Weight (MW)
The mass or formula weight is the sum of monoisotopic masses of all amino acid residues. Calculated by adding atomic masses of all atoms in the backbone and side chains, plus water.
MW = Σ(backbone atoms) + Σ(side chain atoms) + H₂O
Isoelectric Point (pI)
The pH at which the net charge of the peptide is zero. Calculated by assessing partial charges from pH 0 to 14 in 0.01 pH unit increments.
pI = pH where net charge = 0
Net Charge
The sum of positively charged (basic) and negatively charged (acidic) residues at the current pH. Includes contributions from ionizable side chains and termini.
Charge = (+K, +R, +H) + (-D, -E, -C, -Y) + termini
Hydrophobicity
Free energy (ΔG) associated with transitioning the peptide from water to a hydrophobic environment like octanol. Uses the experimentally-determined Wimley-White scale.
Units: kcal/mol
More negative = more hydrophobic
Reference:
S.H. White, W.C. Wimley, "Hydrophobic interactions of peptides with membrane interfaces," Biochimica et Biophysica Acta 1376 (1998) 339-352.
Molar Extinction Coefficient
Describes how much light the peptide absorbs at 280 nm wavelength. The strongly absorbing residues are tryptophan (W), tyrosine (Y), and cysteine (C) when forming disulfide bonds (cystines).
ε₂₈₀ = (W × 5500) + (Y × 1490) + (cystines × 125)
Units: M⁻¹cm⁻¹
Learn more
Chemical Formula
The complete molecular formula showing the total count of each element (C, H, N, O, S) in your peptide.
👀 pH-Dependent Properties

Critical properties such as net charge vary with pH. Use the pH slider to see how your peptide behaves under different conditions. This is especially important for peptides with histidine, aspartic acid, glutamic acid, lysine, arginine, cysteine, or tyrosine residues.

Understanding the Visualization

Chemical Structure Rendering

PepDraw generates professional-quality chemical structures showing the complete peptide backbone and all side chains with proper stereochemistry (line-dash-wedge notation).

pH Effects on Structure

Adjusting the pH slider changes the protonation state of ionizable amino acids:

Basic Residues (gain H⁺)
Lysine (K), Arginine (R), Histidine (H) gain protons to become positively charged at low pH. They lose a proton (becoming neutral) at high pH.
Acidic Residues (lose H⁺)
Aspartic acid (D), Glutamic acid (E) lose protons to become negatively charged at pH > 3.
Special Cases
Cysteine (C) and Tyrosine (Y) lose a proton at high pH to become negatively charged.
Termini
N-terminus is positively charged at low pH. C-terminus is negatively charged at high pH.

Exporting Your Work

Image Formats

PepDraw supports multiple export formats to suit different use cases:

PNG (Raster)
High-resolution bitmap images perfect for presentations, posters, and web use. Images are larger than they appear on-screen for better print quality.
SVG (Vector)
Scalable vector graphics that maintain perfect clarity at any size. Ideal for publications, figures, and professional printing (coming soon as a Pro feature).

Saving Images

💡 Pro Tip

For the highest quality prints, use SVG format when possible. Vector graphics remain sharp at any resolution, making them perfect for journal submissions and large-format posters.

Questions & Support

📧 Get Help

Have questions, feedback, or need assistance with PepDraw? We're here to help!

Email Support
Send your questions or comments to:
support@pepdraw.com
Bug Reports
Found an issue? Please report it with your sequence and browser information so we can investigate.
Feature Requests
Have ideas for new features? We'd love to hear them! Your feedback helps shape PepDraw's development.
Citation Information
Using PepDraw in your research? Contact us for proper citation guidelines and version information.
🎓 Educational Use

Educators: We welcome the use of PepDraw in classroom settings! Let us know if you need any additional features or resources for teaching.

Frequently Asked Questions

Can I use non-standard amino acids?

Currently, PepDraw 4.0 supports the 20 standard amino acids. Support for modified and non-canonical amino acids is planned for future releases.

How accurate are the property calculations?

All calculations use established scientific methods and scales (Wimley-White for hydrophobicity, monoisotopic masses, Henderson-Hasselbalch for pH effects). The values are suitable for research and publication use.

Why does the extinction coefficient show two values?

The first value assumes all cysteines form disulfide bonds (cystines), which contribute 125 M⁻¹cm⁻¹ per pair. The second value assumes all cysteines remain reduced (no disulfides). This gives you both oxidized and reduced scenarios.

What resolution are the exported images?

PNG images are generated at high resolution (typically 300 DPI equivalent) and are larger than they appear on screen. SVG images are vector format and can be scaled to any size without quality loss.

Can I save my sequences for later?

Sequence library features are in development! For now, you can bookmark or copy sequences. Future versions will include user accounts and saved sequence libraries.

Is PepDraw free to use?

Yes! PepDraw's core features are free for academic, educational, and research use. We're developing premium features for advanced users that will be part of a Pro tier.

How do I cite PepDraw in publications?

For citation information, please contact us at support@pepdraw.com. We'll provide you with the appropriate citation format based on your use case.

Tips & Tricks

🎯 Teaching Tip
Use the pH slider interactively to demonstrate acid-base chemistry concepts. Students can see in real-time how ionizable groups respond to pH changes.
📊 Research Tip
Compare similar sequences side-by-side by opening multiple browser tabs. This helps visualize how single mutations affect structure and properties.
🖼️ Presentation Tip
Export structures at different pH values to create before/after comparisons. This is great for illustrating pH-dependent conformational changes.
⚡ Speed Tip
For quick checks, type sequences directly rather than clicking buttons. The interface updates instantly as you type.

Version Information

Current Version: PepDraw 4.0

Complete rebuild with real-time rendering engine, perfect ring geometry for aromatic residues, and enhanced pH-dependent visualization. Built with Python and modern web technologies.

What's New in 4.0

Coming Soon