Abiotic Stress Adaptation: Protein Folding Stability and Dynamics - Abiotic Stress: Plant Responses and Applications in Agriculture - page 19

References
[1] Wang W, Vinocur B, Shoseyov O, Altman A. Role of plant heat-shock proteins and
molecular chaperones in the abiotic stress response. Trends in Plant Science.
2004;9(5) 244-52.
[2] Gaci O, Balev S. A General Model for Amino Acid Interaction Networks. World
Academy of Science, Engineering and Technology. 2008;44 401-405.
[3] Cramer GR, Urano K, Delrot S, Pezzotti M, Shinozaki K. Effects of abiotic stress on
plants: a systems biology perspective. BMC Plant Biology 2011;11 163.
[4] Pain RH. Mechanisms of Protein Folding. Frontiers in Molecular Biology. Oxford
University Press Inc., New York; 2000.
[5] Sadana A, Vo-Dinh T. Biomedical implications of protein folding and misfolding. Bi‐
otechnology and applied biochemistry. 2001;33 7-16.
[6] Kavraki LE. Dimensionality Reduction Methods for Molecular Motion. http://
cnx.org/content/m11461/1.10/. 2007.
[7] Chen P, Long J, Searle MS. Sequential barriers and an obligatory metastable inter‐
mediate define the apparent two-state folding pathway of the ubiquitin-like PB1 do‐
main of NBR1. Journal of Molecular Biology. 2008;376(5) 1463-77.
[8] De Sancho D, Doshi U, Munoz V. Protein folding rates and stability: how much is
there beyond size? Journal of the American Chemical Society. 2009;131(6) 2074-5.
[9] Kjaergaard M, Teilum K, Poulsen FM. Conformational selection in the molten glob‐
ule state of the nuclear coactivator binding domain of CBP. Proceedings of the Na‐
tional Academy of Sciences of the United States of America. 2010;107(28) 12535-40.
[10] Naganathan AN, Doshi U, Fung A, Sadqi M, Munoz V. Dynamics, energetics, and
structure in protein folding. Biochemistry. 2006;45(28) 8466-75.
[11] Farrow NA, Zhang O, Szabo A, Torchia DA, Kay LE. Spectral density function map‐
ping using 15N relaxation data exclusively. Journal of Biomolecular NMR. 1995;6(2)
153-62.
[12] Zhang X, Xu Y, Zhang J, Wu J, Shi Y. Structural and dynamic characterization of the
acid-unfolded state of hUBF HMG box 1 provides clues for the early events in pro‐
tein folding. Biochemistry. 2005;44(22) 8117-25.
[13] Lefevre JF, Dayie KT, Peng JW, Wagner G. Internal mobility in the partially folded
DNA binding and dimerization domains of GAL4: NMR analysis of the N-H spectral
density functions. Biochemistry. 1996;35(8) 2674-86.
[14] Ha JH, Loh SN. Protein Conformational Switches: From Nature to Design. Chemis‐
try-A European Journal. 2012;18(26)7984-99.