Universal Nature of Collapsibility in the Context of Protein Folding and Evolution

被引:28
作者
Thirumalai, D. [1 ]
Samanta, Himadri S. [1 ]
Maity, Hiranmay [2 ]
Reddy, Govardhan [2 ]
机构
[1] Univ Texas Austin, Dept Chem, Austin, TX 78712 USA
[2] Indian Inst Sci, Solid State & Struct Chem Unit, Bangalore 560012, Karnataka, India
基金
美国国家科学基金会;
关键词
SINGLE-MOLECULE FRET; SELF-AVOIDING WALK; RATE-LIMITING STEP; DISORDERED PROTEINS; DENATURED STATE; COLLAPSE; SPECTROSCOPY; SIMULATIONS; DIMENSIONS; SEQUENCES;
D O I
10.1016/j.tibs.2019.04.003
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Theory and simulations predicted that the sizes of the unfolded states of globular proteins should decrease as the denaturant concentration is reduced from a high to a low value. However, small angle X-ray scattering (SAXS) data were used to assert the opposite, while interpretation of single molecule Forster resonance energy transfer experiments (FRET) supported the theoretical predictions. The disagreement between the two experiments is the SAXS-FRET controversy. By harnessing recent advances in SAXS and FRET experiments and setting these findings in the context of a general theory and simulations, which do not rely on experimental data, we establish that compaction of unfolded states under native conditions is universal. The theory also predicts that proteins rich in beta-sheets are more collapsible than alpha-helical proteins. Because the extent of compaction is small, experiments have to be accurate and their interpretations should be as model-free as possible. Theory also suggests that collapsibility itself could be a physical restriction on the evolution of foldable sequences, and also provides a physical basis for the origin of multidomain proteins.
引用
收藏
页码:675 / 687
页数:13
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