About Macromolecular Structure
From Proteopedia
(→A-F - added Extremophiles) |
(→N-R - added nobel prizes) |
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==N-R== | ==N-R== | ||
| + | *[[Nobel Prizes for 3D Molecular Structure]]: The 2009 Nobel Prize in Chemistry for [[Ribosome]] structure is [[Image:New yellow1.gif]]. | ||
*[[Non-Standard Residues]] (see also [[Standard Residues]]) | *[[Non-Standard Residues]] (see also [[Standard Residues]]) | ||
*[[Peptide]] | *[[Peptide]] | ||
Revision as of 12:23, 24 October 2009
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For pages about specific molecules or families of molecules, see Proteopedia:Topic Pages. See also Teaching Strategies Using Proteopedia, and the lists of pages under Research Groups and Institutes and Teaching Scenes, Tutorials, and Educators' Pages. For pages about Proteopedia, its contents, policies, implementation, and credits, see Proteopedia:About. |
Below is a list of pages about macromolecular structure topics. This list excludes pages about specific molecules or families of molecules, and pages in the lists linked in the box at right.
means the article first became available in Proteopedia within the past four months, or that substantial new content was added within the past four months. See also What's New?.
Contents |
A-F
- Activity
- Amino Acids
- Asymmetric Unit
- Atomic Coordinate File
- Believe It or Not
- Biological process
- Biological Unit
- Cellular component
- Classes of globular proteins
- Conservation, Evolutionary
- Domain, protein
- Extremophiles
- Free R
- Function
- Functional annotation
G-M
- Gene
- Highest impact structures
- Hydrogen bonds
- Hydrogen in macromolecular models
- Intrinsically Disordered Protein
- Ligand
- Molecular function
- Molecular modeling and visualization software
- Morphs of conformational changes of macromolecules
N-R
- Nobel Prizes for 3D Molecular Structure: The 2009 Nobel Prize in Chemistry for Ribosome structure is .
- Non-Standard Residues (see also Standard Residues)
- Peptide
- Personal favorites
- PDB file format
- PDB identification code
- Protein Data Bank
- Pyrrolysine, sometimes called the 22nd amino acid
- Quality assessment for molecular models
- R value
- Resolution
- Ramachandran plots
S-Z
- Selenocysteine, the 21st amino acid
- Single protein
- Sites, Functional
- Software for molecular modeling and visualization
- Standard Residues (see also Non-Standard Residues)
- Structural annotation
- Teaching Strategies Using Proteopedia
- Temperature value
- X-ray crystallography
Proteopedia Page Contributors and Editors (what is this?)
Eric Martz, Wayne Decatur, Joel L. Sussman, Alejandro Porto, Angel Herraez, Eran Hodis
