This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
Search results
From Proteopedia
You searched for Backside
There is no page with the exact title "Backside". The search results for "Backside" are displayed below. You can create a page titled Backside (by clicking on the red link).
For more information about searching Proteopedia, see Help.
To exclude pages titled with 4-character PDB codes, use the checkbox "only Human created pages" at the bottom of this page.
Showing below up to 20 results starting with #1.
View (previous 20) (next 20) (20 | 50 | 100 | 250 | 500)
Article title matches
- Category:In-line backside nucleophilic substitution (73 bytes)
1: List of pages with the keyword In-line backside nucleophilic substitution - Category:Backside (39 bytes)
1: List of pages with the keyword Backside
Page text matches
- 2zoq (6,836 bytes)
24: ...ifferences in the D-motif binding site and in the backside binding site are putative targets for development... - 4jh8 (4,951 bytes)
14: ...solvent channel, where the thiol has added to the backside of fosfomycin C1 located at the end of the channe... - 2rii (4,702 bytes)
24: ...minus of Prx, and its unexpected packing onto the backside of Srx away from the Srx active site. Binding stu... - 2r0k (4,766 bytes)
23: ...sites (S3 and S2). In contrast, Ab75 bound at the backside of the cleft to a region corresponding to thrombi... - 2r0l (5,103 bytes)
24: ...sites (S3 and S2). In contrast, Ab75 bound at the backside of the cleft to a region corresponding to thrombi... - 3dae (4,816 bytes)
23: ...s cerevisiae (Snf1-pKD). The AID binds, from the 'backside', to the hinge region of its kinase domain, formi... - 3h4j (4,532 bytes)
23: ...s cerevisiae (Snf1-pKD). The AID binds, from the 'backside', to the hinge region of its kinase domain, formi... - 3h7d (5,516 bytes)
26: ...multiple contacts with amino acid residues on the backside of the catK molecule that help to facilitate comp... - 3a33 (4,816 bytes)
24: ... is assembled into an infinite spiral through the backside interaction. This active complex may provide mult... - T4 RNA ligase 2 (Rnl2) (10,135 bytes)
19: ...plishes this structural function by tethering the backside of the motif I loop (green) to the start of<scene... - 2yb6 (4,072 bytes)
14: ...ty by competing with ubiquitin for a noncovalent "backside" binding site on Rad6. Our findings provide mecha... - Ionotropic Glutamate Receptors (11,858 bytes)
46: ...tamate_Receptors/Locked_into_place/2'>bind on the backside</scene> ([[2al4]]) of the ligand-binding core thr... - 2ybf (4,236 bytes)
14: ...ty by competing with ubiquitin for a noncovalent "backside" binding site on Rad6. Our findings provide mecha... - 4jqu (4,500 bytes)
14: ...alpha-helices that interact extensively with the "backside" of Ubc7p. Residues essential for E2 binding are ... - 4ky1 (3,667 bytes)
11: ...murine, or by mutating some residues on the CDRs' backside to human or to a de novo designed sequence. The f... - Fatty acid amide hydrolase (13,090 bytes)
17: ...substrate. Flaps 1 and 2 envelope the middle and backside of the anandamide mimic, and are locked together ... - Sandbox Reserved 921 (5,529 bytes)
27: ...substrate. Flaps 1 and 2 envelope the middle and backside of the anandamide mimic, and are locked together ... - Sandbox Reserved 922 (2,698 bytes)
13: ...substrate. Flaps 1 and 2 envelope the middle and backside of the anandamide mimic, and are locked together ... - 4r62 (4,797 bytes)
14: ... and reveal new ways in which contacts with an E2 backside can regulate ubiquitin conjugating activity. - 4v3k (4,510 bytes)
14: ...the mechanism remains elusive. Here, we show that backside bound Ub (UbB) enhances both RING-independent and...
View (previous 20) (next 20) (20 | 50 | 100 | 250 | 500)
You may also try
