Substitutions of Amino Acids with Large Number of Contacts in the Native State Have no Effect on the Rates of Protein Folding
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- 作者：Bogdan S. Melnika ; bmelnik@phys.protres.ru" class="auth_mail" title="E-mail the corresponding author ; Galina S. Nagibinaa ; Anatoly S. Glukhova ; Tatiana N. Melnika ; Vladimir N. Uverskyb ; c ; vuversky@health.usf.edu" class="auth_mail" title="E-mail the corresponding author
- 关键词：Point amino acid substitutions ; Protein folding rate ; Protein unfolding rate ; Protein folding transition state ; carbonic anhydrase II
- 刊名：Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
- 出版年：2016
- 出版时间：December 2016
- 年：2016
- 卷：1864
- 期：12
- 页码：1809-1817
- 全文大小：784 K
文摘
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A rule is proposed on the effects of mutations of highly connected residues
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Mutations of highly connected hydrophobic residues should affect unfolding rates
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Such mutations would not change the folding rates of a protein
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Experimental support of this hypothesis is provided
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This rule can facilitate the work on constructing mutant forms of proteins