Abstract
The first comprehensive studies on the structure and thermodynamics of membrane proteins have started revealing the exact architecture of these macromolecules and the physical-chemical rules behind their structures. In this review, the stabilities of several families of membrane proteins, obtained by using spectroscopic, calorimetric and single molecule techniques are surveyed. The data on the stability of membrane proteins are compared with those obtained in soluble proteins. The comparison indicates that although the number of particular atomic interactions is larger in membrane proteins than in soluble ones, the overall values are similar. The consensus is that some intrinsic properties of membrane proteins resemble those of soluble ones, but there are critical differences arising form the inter-molecular contacts with the surrounding membrane. Taken together, all these efforts improve our understanding of the universal forces governing protein folding, and will help in the design of membrane proteins in the near future.
Keywords: Lipids, proteins, thermodynamics, spectroscopy, SDS, alcohols, stability
Current Protein & Peptide Science
Title: Into the Lipid Realm: Stability and Thermodynamics of Membrane Proteins
Volume: 9 Issue: 6
Author(s): Francisco N. Barrera, Luis A. Alcaraz, Estefania Hurtado-Gomez and Jose L. Neira
Affiliation:
Keywords: Lipids, proteins, thermodynamics, spectroscopy, SDS, alcohols, stability
Abstract: The first comprehensive studies on the structure and thermodynamics of membrane proteins have started revealing the exact architecture of these macromolecules and the physical-chemical rules behind their structures. In this review, the stabilities of several families of membrane proteins, obtained by using spectroscopic, calorimetric and single molecule techniques are surveyed. The data on the stability of membrane proteins are compared with those obtained in soluble proteins. The comparison indicates that although the number of particular atomic interactions is larger in membrane proteins than in soluble ones, the overall values are similar. The consensus is that some intrinsic properties of membrane proteins resemble those of soluble ones, but there are critical differences arising form the inter-molecular contacts with the surrounding membrane. Taken together, all these efforts improve our understanding of the universal forces governing protein folding, and will help in the design of membrane proteins in the near future.
Export Options
About this article
Cite this article as:
Barrera N. Francisco, Alcaraz A. Luis, Hurtado-Gomez Estefania and Neira L. Jose, Into the Lipid Realm: Stability and Thermodynamics of Membrane Proteins, Current Protein & Peptide Science 2008; 9 (6) . https://dx.doi.org/10.2174/138920308786733949
DOI https://dx.doi.org/10.2174/138920308786733949 |
Print ISSN 1389-2037 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5550 |
Call for Papers in Thematic Issues
Advancements in Proteomic and Peptidomic Approaches in Cancer Immunotherapy: Unveiling the Immune Microenvironment
The scope of this thematic issue centers on the integration of proteomic and peptidomic technologies into the field of cancer immunotherapy, with a particular emphasis on exploring the tumor immune microenvironment. This issue aims to gather contributions that illustrate the application of these advanced methodologies in unveiling the complex interplay ...read more
Nutrition and Metabolism in Musculoskeletal Diseases
The musculoskeletal system consists mainly of cartilage, bone, muscles, tendons, connective tissue and ligaments. Balanced metabolism is of vital importance for the homeostasis of the musculoskeletal system. A series of musculoskeletal diseases (for example, sarcopenia, osteoporosis) are resulted from the dysregulated metabolism of the musculoskeletal system. Furthermore, metabolic diseases (such ...read more
Protein Folding, Aggregation and Liquid-Liquid Phase Separation
Protein folding, misfolding and aggregation remain one of the main problems of interdisciplinary science not only because many questions are still open, but also because they are important from the point of view of practical application. Protein aggregation and formation of fibrillar structures, for example, is a hallmark of a ...read more
Related Journals
- Author Guidelines
- Graphical Abstracts
- Fabricating and Stating False Information
- Research Misconduct
- Post Publication Discussions and Corrections
- Publishing Ethics and Rectitude
- Increase Visibility of Your Article
- Archiving Policies
- Peer Review Workflow
- Order Your Article Before Print
- Promote Your Article
- Manuscript Transfer Facility
- Editorial Policies
- Allegations from Whistleblowers