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Literature DB >> 19174518

Waltzing alpha-helices.

Victor Muñoz¹, Ravishankar Ramanathan.

Abstract

Mesh：

Year: 2009 PMID： 19174518 PMCID： PMC2635837 DOI： 10.1073/pnas.0812577106

Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205

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12 in total

Review 1. Fast kinetics and mechanisms in protein folding.

Authors: W A Eaton; V Muñoz; S J Hagen; G S Jas; L J Lapidus; E R Henry; J Hofrichter
Journal: Annu Rev Biophys Biomol Struct Date: 2000

2. Time-resolved infrared study of the helix-coil transition using (13)C-labeled helical peptides.

Authors: C Y Huang; Z Getahun; T Wang; W F DeGrado; F Gai
Journal: J Am Chem Soc Date: 2001-12-05 Impact factor: 15.419

3. Measuring dynamic flexibility of the coil state of a helix-forming peptide.

Authors: Lisa J Lapidus; William A Eaton; James Hofrichter
Journal: J Mol Biol Date: 2002-05-24 Impact factor: 5.469

4. Local conformational dynamics in alpha-helices measured by fast triplet transfer.

Authors: Beat Fierz; Andreas Reiner; Thomas Kiefhaber
Journal: Proc Natl Acad Sci U S A Date: 2009-01-08 Impact factor: 11.205

Review 5. Helix design, prediction and stability.

Authors: V Muñoz; L Serrano
Journal: Curr Opin Biotechnol Date: 1995-08 Impact factor: 9.740

Review 6. Stability of alpha-helices.

Authors: A Chakrabartty; R L Baldwin
Journal: Adv Protein Chem Date: 1995

7. Fast events in protein folding: helix melting and formation in a small peptide.

Authors: S Williams; T P Causgrove; R Gilmanshin; K S Fang; R H Callender; W H Woodruff; R B Dyer
Journal: Biochemistry Date: 1996-01-23 Impact factor: 3.162

8. Elucidating the folding problem of helical peptides using empirical parameters.

Authors: V Muñoz; L Serrano
Journal: Nat Struct Biol Date: 1994-06

9. Kinetics of the helix-coil transition of a polypeptide with non-ionic side groups, derived from ultrasonic relaxation measurements.

Authors: B Gruenewald; C U Nicola; A Lustig; G Schwarz; H Klump
Journal: Biophys Chem Date: 1979-01 Impact factor: 2.352

6. Spectroscopic Investigation of the Kinetic Mechanism Involved in the Association of Potyviral VPg with the Host Plant Translation Initiation Factor eIF4E.

Authors: Jocelyne Walter; Amandine Barra; Justine Charon; Geneviève Tavert-Roudet; Thierry Michon
Journal: Int J Mol Sci Date: 2020-08-05 Impact factor: 5.923

6 in total

Waltzing alpha-helices.

Review 1. Fast kinetics and mechanisms in protein folding.

2. Time-resolved infrared study of the helix-coil transition using (13)C-labeled helical peptides.

3. Measuring dynamic flexibility of the coil state of a helix-forming peptide.

4. Local conformational dynamics in alpha-helices measured by fast triplet transfer.

Review 5. Helix design, prediction and stability.

Review 6. Stability of alpha-helices.

7. Fast events in protein folding: helix melting and formation in a small peptide.

8. Elucidating the folding problem of helical peptides using empirical parameters.

9. Kinetics of the helix-coil transition of a polypeptide with non-ionic side groups, derived from ultrasonic relaxation measurements.

10. A salt bridge stabilizes the helix formed by isolated C-peptide of RNase A.

1. Structure and mechanism of maximum stability of isolated alpha-helical protein domains at a critical length scale.

2. Direct evidence for a dry molten globule intermediate during the unfolding of a small protein.

3. Structure fluctuations and conformational changes in protein binding.

4. Kinks, loops, and protein folding, with protein A as an example.

Review 5. When fast is better: protein folding fundamentals and mechanisms from ultrafast approaches.

6. Spectroscopic Investigation of the Kinetic Mechanism Involved in the Association of Potyviral VPg with the Host Plant Translation Initiation Factor eIF4E.