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The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis
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The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis

Published on: March 17, 2010

Analysis of side chain mobility among protein G B1 domain mutants with widely varying stabilities

Virginia A Goehlert1, Ewa Krupinska, Lynne Regan

  • 1Department of Chemistry, Indiana University, Bloomington, Indiana 47405-0001, USA.

Protein Science : a Publication of the Protein Society
|November 13, 2004
PubMed

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Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
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Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
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Conservation of Protein Domains

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Ligand Binding and Linkage

Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence the...