Warning: Undefined array key "mm" in /www/wwwroot/www.ai-bt.com/si.php on line 10 Deprecated: trim(): Passing null to parameter #1 ($string) of type string is deprecated in /www/wwwroot/www.ai-bt.com/si.php on line 10 Toward a proper interpretation of hydrogen exchange data in disordered proteins.

Literature DB >> 34416173

Toward a proper interpretation of hydrogen exchange data in disordered proteins.

Nikolai R Skrynnikov¹.

Abstract

Entities: Chemical

Mesh：

Substances：
Proteins
Hydrogen

Year: 2021 PMID： 34416173 PMCID： PMC8510856 DOI： 10.1016/j.bpj.2021.08.004

Source DB: PubMed Journal: Biophys J ISSN： 0006-3495 Impact factor: 3.699

Keyword Cloud
References

× No keyword cloud information.

11 in total

1. A Gaussian-chain model for treating residual charge-charge interactions in the unfolded state of proteins.

Authors: Huan-Xiang Zhou
Journal: Proc Natl Acad Sci U S A Date: 2002-03-12 Impact factor: 11.205

2. Sequence determinants of compaction in intrinsically disordered proteins.

Authors: Joseph A Marsh; Julie D Forman-Kay
Journal: Biophys J Date: 2010-05-19 Impact factor: 4.033

3. Structural differences in Abeta amyloid protofibrils and fibrils mapped by hydrogen exchange--mass spectrometry with on-line proteolytic fragmentation.

Authors: Indu Kheterpal; Maolian Chen; Kelsey D Cook; Ronald Wetzel
Journal: J Mol Biol Date: 2006-07-12 Impact factor: 5.469

4. Distinct aggregation mechanisms of monoclonal antibody under thermal and freeze-thaw stresses revealed by hydrogen exchange.

Authors: Aming Zhang; Satish K Singh; Michael R Shirts; Sandeep Kumar; Erik J Fernandez
Journal: Pharm Res Date: 2011-07-30 Impact factor: 4.200

5. Remaining structures at the N- and C-terminal regions of alpha-synuclein accurately elucidated by amide-proton exchange NMR with fitting.

Authors: Honoka Okazaki; Yuka Ohori; Masaya Komoto; Young-Ho Lee; Yuji Goto; Naoya Tochio; Chiaki Nishimura
Journal: FEBS Lett Date: 2013-10-07 Impact factor: 4.124

Toward a proper interpretation of hydrogen exchange data in disordered proteins.

1. A Gaussian-chain model for treating residual charge-charge interactions in the unfolded state of proteins.

2. Sequence determinants of compaction in intrinsically disordered proteins.

3. Structural differences in Abeta amyloid protofibrils and fibrils mapped by hydrogen exchange--mass spectrometry with on-line proteolytic fragmentation.

4. Distinct aggregation mechanisms of monoclonal antibody under thermal and freeze-thaw stresses revealed by hydrogen exchange.

5. Remaining structures at the N- and C-terminal regions of alpha-synuclein accurately elucidated by amide-proton exchange NMR with fitting.

6. Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseH.

7. Hydrogen exchange identifies native-state motional domains important in protein folding.

8. Measuring hydrogen exchange rates in invisible protein excited states.

9. Bacterial inclusion bodies contain amyloid-like structure.

10. The contribution of electrostatics to hydrogen exchange in the unfolded protein state.