From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:3al1.jpg|left|200px]] | + | {{Seed}} |
| | + | [[Image:3al1.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_3al1| PDB=3al1 | SCENE= }} | | {{STRUCTURE_3al1| PDB=3al1 | SCENE= }} |
| | | | |
| - | '''DESIGNED PEPTIDE ALPHA-1, RACEMIC P1BAR FORM'''
| + | ===DESIGNED PEPTIDE ALPHA-1, RACEMIC P1BAR FORM=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | We report the 0.75 A crystal structure of a racemic mixture of the 12-residue designed peptide "Alpha-1" (Acetyl-ELLKKLLEELKG), the L-enantiomer of which is described in the accompanying paper. Equivalent solutions of the centrosymmetric bilayers were determined by two direct phasing programs in space groups P1 and P1bar. The unit cell contains two L-alpha-helices and two D-alpha-helices. The columnar-sheet bilayer motif seen in L-Alpha-1 is maintained in the D,L-Alpha-1 structure except that each sheet of head-to-tail helices is composed of one enantiomer and is related to its neighboring sheets by inversion symmetry. Comparison to the L-Alpha-1 structure provides further insight into peptide design. The high resolution and small asymmetric unit allowed building an intricate model (R = 13.1%, Rfree = 14.5%) that incorporates much of the discrete disorder of peptide and solvent. Ethanolamine and 2-methyl-2,4-pentanediol (MPD) molecules bind near helix termini. Rigid body analysis identifies sites of restricted displacements and torsions. Side-chain discrete disorder propagates into the backbone of one helix but not the other. Although no side chain in Alpha-1 is rigid, the environments in the crystal restrict some of them to no or only one active torsion.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_10422829}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10422829 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_10422829}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 29: |
Line 33: |
| | [[Category: Helical bilayer]] | | [[Category: Helical bilayer]] |
| | [[Category: Racemic]] | | [[Category: Racemic]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 20:19:21 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:01:00 2008'' |
Revision as of 13:01, 27 July 2008
Template:STRUCTURE 3al1
DESIGNED PEPTIDE ALPHA-1, RACEMIC P1BAR FORM
Template:ABSTRACT PUBMED 10422829
About this Structure
Full crystallographic information is available from OCA.
Reference
Centrosymmetric bilayers in the 0.75 A resolution structure of a designed alpha-helical peptide, D,L-Alpha-1., Patterson WR, Anderson DH, DeGrado WF, Cascio D, Eisenberg D, Protein Sci. 1999 Jul;8(7):1410-22. PMID:10422829
Page seeded by OCA on Sun Jul 27 16:01:00 2008
