𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Functional significance of flexibility in proteins

✍ Scribed by Robert Huber; William S. Bennett Jr.

Publisher
Wiley (John Wiley & Sons)
Year
1983
Tongue
English
Weight
946 KB
Volume
22
Category
Article
ISSN
0006-3525

No coin nor oath required. For personal study only.

✦ Synopsis

Institut f u r Biochemie, 0-8033 Martinsried bei Muenchen, Federal

Republic of Germany

Synopsis

The structural basis and the functional implications of large-scale flexibility are discussed for three systems: trypsin-trypsinogen, immunoglobulins, and citrate synthase. The trypsin-trypsinogen system provides an example in which an order-disorder transition is used as a means to regulate enzymatic activity. Immunoglobulins demonstrate how flexibly linked domains may be used to allow the binding of ligands with diverse arrangements. In citrate synthase, domain motion forms an active site that is shielded from solvent. Analogous large-scale flexibility has been observed in a number of other systems. 13,222.

πŸ“œ SIMILAR VOLUMES

MCSS functionality maps for a flexible p
MCSS functionality maps for a flexible protein
✍ Collin M. Stultz; Martin Karplus πŸ“‚ Article πŸ“… 1999 πŸ› John Wiley and Sons 🌐 English βš– 480 KB

The Multiple Copy Simultaneous Search (MCSS) methodology for finding energetically favorable positions and orientations of small functional groups in a binding site is extended to include flexibility of the target. This makes possible the finding of novel minima not present in a fixed structure and

Side-chain flexibility in proteins upon
Side-chain flexibility in proteins upon ligand binding
✍ Rafael Najmanovich; Josef Kuttner; Vladimir Sobolev; Marvin Edelman πŸ“‚ Article πŸ“… 2000 πŸ› John Wiley and Sons 🌐 English βš– 122 KB πŸ‘ 1 views

Ligand binding may involve a wide range of structural changes in the receptor protein, from hinge movement of entire domains to small side-chain rearrangements in the binding pocket residues. The analysis of side chain flexibility gives insights valuable to improve docking algorithms and can provide

Conformational selection of protein kina
Conformational selection of protein kinase A revealed by flexible-ligand flexible-protein docking
✍ Zunnan Huang; Chung F. Wong πŸ“‚ Article πŸ“… 2009 πŸ› John Wiley and Sons 🌐 English βš– 919 KB

## Abstract Protein kinases have high structural plasticity: their structure can change significantly, depending on what ligands are bound to them. Rigid‐protein docking methods are not capable of describing such effects. Here, we present a new flexible‐ligand flexible‐protein docking model in whic