Related Experiment Video
Updated: Sep 21, 2026

Examining the Conformational Dynamics of Membrane Proteins in situ with Site-directed Fluorescence Labeling
Published on: May 29, 2011
Theory of large-amplitude conformational fluctuations in native globular proteins. Independent fluctuating site model
Abstract:
A theory is developed about large-amplitude conformational fluctuations in globular proteins in their native or predenaturational state. A model is introduced, an independent fluctuating site model, in which we assume that there is more than one independent fluctuating site, each one localized in some part of a protein molecule. Without assuming any further details for each fluctuating site, the entropy S versus enthalpy H curve of this model is shown to be convex. From this fact the predenaturational excess heat capacity can be derived, as observed in recent experimental studies of a few systems of a protein in solution.
Related Concept Videos
Protein Folding
Protein Folding
Globular and Fibrous Proteins
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
Cooperative Allosteric Transitions
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Globular and Fibrous Proteins
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...

