Structural Biology: Scientific Figures & Vector Diagrams

The molecular machinery of the central dogma governs genetic storage, replication, transcription, and translation in living systems.

Biophysical techniques utilize physical principles of electromagnetism, thermodynamics, and optics to probe biomolecular structure and dynamics.

Protein folding is a stochastic process in which the denaturated polypeptide chain (D) explores many different conformations associated with different free energy. As water flowing downhill, proteins fold by following the shortest path to the conformation endowed with the lowest free energy: the native state (N)

This detailed scientific diagram illustrates Protein Ribbon (Nih Bioart 727 791019) in the context of Structural Biology.

This detailed scientific diagram illustrates Protein Backbone Phipsiomega in the context of Structural Biology.

Schematic diagram of antiparallel hydrogen bonding in the beta sheet protein structural motif . Created using ACD/ChemSketch 10.0 and Inkscape . Legend Oxygen atoms Nitrogen atoms

This graphic shows how different gene regulatory factors contact their nucleic acid targets and roughly the size of their binding sites. Transcription factors binding to DNA, RNA-binding proteins and a microRNA binding to RNA. In grey: four types of DNA binding domains on the left (zinc finger, homeodomain, helix-loop-helix, forkhead)( PDB : 6ML2 , 6KKS , 1NKP , 3G73 ​), two types of RNA-binding domains in the middle (RNA recognition motif, KH-domain) binding different target mRNAs in various ways ( PDB : 4BS2 , 6GBM , 5MPG , 5O1Z , 1EC6 , 4JVH ​), and on the right a microRNA in light blue, in complex with the Argonaute protein, bound to a target mRNA ( PDB : 6MDZ ​).

Ramachandran plots of protein phi,psi backbone dihedral angles, for the six distinct amino-acid categories used in model validation at the worldwide Protein Data Bank since 2013. Data from about 1.5 million quality-filtered residues; contours from MolProbity. Inner contour encloses the "favored" region that includes 98% of the high-quality reference data; outer dark contour divides the "outlier" region from the "allowed" region.

A Ramachandran plot of the phi,psi protein backbone dihedral angles for Glycine, from a dataset of 1.5 million residues in 8000 protein chains with resolution <2.0Å and backbone B-factors ≤30. The 116,789 individual-residue datapoints are color-coded by the number in each 0.1° bin. The inner contour encloses 98% of the data (the "favored" region, while the outer contour encloses 99.9% of the data, dividing "allowed" from "outlier" regions.

Crystal structure of the soluble peridinin-chlorophyll-protein complex from the photosynthetic dinoflagellate Amphidinium carterae , showing the noncrystallographic trimer consistent with biochemical observations about the natural oligomer state. This complex is found in many photosynthetic dinoflagellates and involves a boat or cradle-shaped protein with two pseudosymmetrical repeats of eight alpha helices (shown in the lower left monomer in blue and orange) wrapped around a pigment-filled central cavity. Each eight-helix segment binds one chlorophyll molecule (green, with central magnesium ion shown as a green sphere), one diacylglycerol molecule (yellow) and four peridinin molecules (gray). For the other two monomers, only the protein is shown, in tan and red. Compare File:1ppr peridinin chlorophyll protein.png , which shows only the lower left monomer in a similar orientation. Rendered using PyMol from PDB ID 1PPR. Hofmann E, Wrench PM, Sharples FP, Hiller RG, Welte W, Diederichs K. Structural basis of light harvesting by carotenoids: peridinin-chlorophyll-protein from Amphidinium carterae. Science. 1996;272(5269):1788-91. DOI 10.1126/science.272.5269.1788.

Shows the hydrophobic and hydrophilic orientations of the alpha helix domains for TMEM241 Isoform 1

An example of a 4-stranded antiparallel β sheet fragment from a crystal structure of the enzyme catalase (PDB file 1GWE at 0.88 Å resolution). a) Front view, showing the antiparallel hydrogen bonds (dotted) between peptide NH and CO groups on adjacent strands. Arrows indicate chain direction, and electron density contours outline the non-H atoms. O atoms are red balls, N atoms are blue, and H atoms are omitted for simplicity; sidechains are shown only out to the first sidechain C atom (green). b) Edge-on view of the central two β strands in a, showing the righthanded twist and the pleat of Cαs and sidechains that alternately stick out in opposite directions from the sheet.

Diagram of beta-Pleated sheet structure of protein en:User talk:G3pro#Image source

Cartoon representation of the molecular structure of protein registered with 2yrk code.

Cartoon representation of a complex between DNA and the ZIF268 protein, containing 3 zinc finger motifs. The coordinating residues of the middle zinc finger are highlighted. Based on the x-ray structure of PDB 1A1L. Color coding: ZIF268: blue; DNA: orange; Zinc ions: green