The hydrophobic effect: A new insight from cold denaturation and a two-state water structure

Critical Reviews in Biochemistry and Molecular Biology

Volumn 37, Issue 2, 2002, Pages 55-69

  Tsai, Chung Jung ^a   Maizel, Jacob V ^b   Nussinov, Ruth ^a,c  

^a SAIC FREDERICK INC   (United States)

^b NATIONAL CANCER INSTITUTE   (United States)

^c TEL AVIV UNIVERSITY   (Israel)

Author keywords

lactalbumin; Cold denaturation; Entropy; Hydrophobic effect; Molecular simulations; Molten globule; Water structure

Indexed keywords

DENATURATION; ENERGY; ENTHALPY; ENTROPY; HYDROPHOBICITY; MOLECULAR DYNAMICS; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; REVIEW; TEMPERATURE DEPENDENCE; THERMODYNAMICS; WATER STRUCTURE; CHEMISTRY; COLD; HEAT; METABOLISM; PHYSIOLOGY; PROTEIN DENATURATION; PROTEIN ENGINEERING;

LACTALBUMIN; WATER;

COLD; ENTROPY; HEAT; HYDROPHOBICITY; LACTALBUMIN; PROTEIN DENATURATION; PROTEIN ENGINEERING; PROTEIN FOLDING; WATER;

EID: 0036252440     PISSN: 10409238     EISSN: None     Source Type: Journal    
DOI: 10.1080/10409230290771456     Document Type: Review

References (22)

1. Cold denaturation of proteins
2. Properties of liquid water: Origin of the density anomalies
3. A simple model of water and the hydrophobic effect
4. Some factors in the interpretation of protein denaturation
5. Temperature, Stability, and the hydrophobic interaction
6. Dominant forces in protein folding
7. Navigating the folding routes
8. Rapid collapse and slow structural reorganization during the refolding of bovine α-lactalbumin
9. Anatomy of protein structures: Visualizing how a 1D protein chain folds into a 3D shape
10. Transient, highly populated, building blocks folding model
11. Energetic basis of structural stability in the molten globule state: A-lactalbumin
12. Protein heat capacity: Inconsistencies in the current view of cold denaturation
13. The hydrophobic effect. I. A consequence of the mobile order in H-bonded liquids
14. The molten globule state as a clue for understanding the folding and cooperativity of globular protein structure
15. α-lactalbumin: Structure and function
16. Differences in the processes of b-lactoglobulin cold and heat denaturations
17. Cold denaturation of α-lactalbumin
18. Conformational stability of the Escherichia coli HPr protein: Test of the linear extrapolation method and a thermodynamic characterization of cold denaturation
19. Cold denaturation of monomeric peptide helices
20. A reassessment of the molecular origin of cold denaturation
21. Role of hydration water in protein unfolding
22. Thermodynamic differences among homologous thermophilic and mesophilic proteins