Book chapter
Fine-Tuning Protein Stability
Water and Life: The Unique Properties of H2O, pp.189-202
CRC Press
2010
DOI: 10.1201/EBK1439803561
Abstract
In all living systems, proteins perform the tasks that make life possible. To carry out their biological functions, the chain of amino acids making up the protein must fold, in the presence of water, to a unique, three-dimensional structure called the native state. These proteins are called globular proteins and they are, by far, the most abundant class of proteins. Sometimes, proteins have more than one globular unit in a single polypeptide chain and these units are then called domains. Other times, these globular units associate noncovalently to form larger proteins and this assembly and its architecture is called quaternary structure. Here, we will focus our attention on two proteins that differ markedly in size but fold to give a single globular unit. We are most interested in the forces that determine the stability of this tertiary structure of globular proteins (Petsko and Ringe, 2004).
Details
- Title: Subtitle
- Fine-Tuning Protein Stability
- Creators
- Carlos Warnick Pace - Texas A&M Univ, Dept Biochem & Biophys, College Stn, TX 77843 USAAbbas Razvi - Scripps Research InstituteJ. Martin Scholtz - Texas A&M Univ, College Stn, TX USA
- Contributors
- Ruth M Lynden-Bell (Editor)Simon Conway Morris (Editor)John D Barrow (Editor)John L Finney (Editor)Charles Harper (Editor)
- Resource Type
- Book chapter
- Publication Details
- Water and Life: The Unique Properties of H2O, pp.189-202
- DOI
- 10.1201/EBK1439803561
- Publisher
- CRC Press; Boca Raton, Florida
- Number of pages
- 14
- Language
- English
- Date published
- 2010
- Academic Unit
- Research Administration; Pharmaceutical Sciences and Experimental Therapeutics; Biochemistry and Molecular Biology; Chemistry
- Record Identifier
- 9984293415202771
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