Structural basis for unfolding pathway-dependent stability of proteins: Vectorial unfolding versus global unfolding
نویسندگان
چکیده
منابع مشابه
Slow Unfolding of Monomeric Proteins from Hyperthermophiles with Reversible Unfolding
Based on the differences in their optimal growth temperatures microorganisms can be classified into psychrophiles, mesophiles, thermophiles, and hyperthermophiles. Proteins from hyperthermophiles generally exhibit greater stability than those from other organisms. In this review, we collect data about the stability and folding of monomeric proteins from hyperthermophilies with reversible unfold...
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Thermal unfolding of proteins is compared to folding and mechanical stretching in a simple topology-based dynamical model. We define the unfolding time and demonstrate its low-temperature divergence. Below a characteristic temperature, contacts break at separate time scales and unfolding proceeds approximately in a way reverse to folding. Features in these scenarios agree with experiments and a...
متن کاملTemperature dependent protein unfolding
Protein structure prediction is a central problem in current biophysics. Understanding the energy landscape roughness would shed light on the physics behind protein folding. The theory for extracting energy landscape roughness from temperature dependent unfolding measurements is reviewed. Improvements facilitating temperature dependent single molecule protein unfolding experiments are described...
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The biophysical characterization of integral membrane protein stability is often challenging due to several factors: First, the expression and purification of membrane proteins is often impeded by low expression levels and protein stability. As a result, yields are usually low and do not allow for a thorough analysis or a screening approach to determine optimal conditions. Second, the use of de...
متن کاملForce induced unfolding of proteins
Native structures of wild-type proteins may unfold as external conditions change. Usually unfolding occurs as a result of raising temperature, increasing the concentration of denaturants such as urea or guanidinium chloride, or changing pH. Only recently it has been recognized that certain wild-type proteins are subject to external force and in the course of performing biological functions they...
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ژورنال
عنوان ژورنال: Protein Science
سال: 2010
ISSN: 0961-8368
DOI: 10.1002/pro.346