Literature DB >> 32029956

Ultraviolet Resonance Raman Spectroscopic Markers for Protein Structure and Dynamics.

Ryan S Jakubek1, Joseph Handen2, Stephen E White1,3, Sanford A Asher1, Igor K Lednev2.   

Abstract

UV resonance Raman (UVRR) spectroscopy is a powerful tool for investigating the structure of biological molecules, such as proteins. Numerous UVRR spectroscopic markers that provide information on the structure and environment of the protein backbone and of amino acid side chains have recently been discovered. Combining these UVRR markers with hydrogen-deuterium exchange and advanced statistics is a powerful tool for studying protein systems, including the structure and formation mechanism of protein aggregates and amyloid fibrils. These techniques allow crucial new insights into the structure and dynamics of proteins, such as polyglutamine peptides, which are associated with 10 different neurodegenerative diseases. Here we summarize the spectroscopic structural markers recently developed and the important insights they provide.

Entities:  

Keywords:  Fibrils; Polyglutamine; Raman; UVRR

Year:  2017        PMID: 32029956      PMCID: PMC7003616          DOI: 10.1016/j.trac.2017.12.002

Source DB:  PubMed          Journal:  Trends Analyt Chem        ISSN: 0165-9936            Impact factor:   12.296


  41 in total

Review 1.  Comparison of protein structures determined by NMR in solution and by X-ray diffraction in single crystals.

Authors:  M Billeter
Journal:  Q Rev Biophys       Date:  1992-08       Impact factor: 5.318

2.  Structural variations in the cross-beta core of amyloid beta fibrils revealed by deep UV resonance Raman spectroscopy.

Authors:  Ludmila A Popova; Ravindra Kodali; Ronald Wetzel; Igor K Lednev
Journal:  J Am Chem Soc       Date:  2010-05-12       Impact factor: 15.419

3.  Genetic engineering combined with deep UV resonance Raman spectroscopy for structural characterization of amyloid-like fibrils.

Authors:  Vitali Sikirzhytski; Natalya I Topilina; Seiichiro Higashiya; John T Welch; Igor K Lednev
Journal:  J Am Chem Soc       Date:  2008-04-15       Impact factor: 15.419

4.  UV resonance Raman determination of protein acid denaturation: selective unfolding of helical segments of horse myoglobin.

Authors:  Z Chi; S A Asher
Journal:  Biochemistry       Date:  1998-03-03       Impact factor: 3.162

5.  Spontaneous inter-conversion of insulin fibril chirality.

Authors:  Dmitry Kurouski; Rina K Dukor; Xuefang Lu; Laurence A Nafie; Igor K Lednev
Journal:  Chem Commun (Camb)       Date:  2012-01-12       Impact factor: 6.222

6.  Glutamine and Asparagine Side Chain Hyperconjugation-Induced Structurally Sensitive Vibrations.

Authors:  David Punihaole; Zhenmin Hong; Ryan S Jakubek; Elizabeth M Dahlburg; Steven Geib; Sanford A Asher
Journal:  J Phys Chem B       Date:  2015-09-30       Impact factor: 2.991

Review 7.  UV resonance Raman spectroscopy for analytical, physical, and biophysical chemistry. Part 2.

Authors:  S A Asher
Journal:  Anal Chem       Date:  1993-02-15       Impact factor: 6.986

Review 8.  UV resonance Raman investigations of peptide and protein structure and dynamics.

Authors:  Sulayman A Oladepo; Kan Xiong; Zhenmin Hong; Sanford A Asher; Joseph Handen; Igor K Lednev
Journal:  Chem Rev       Date:  2012-02-15       Impact factor: 60.622

9.  Polyglutamine Fibrils: New Insights into Antiparallel β-Sheet Conformational Preference and Side Chain Structure.

Authors:  David Punihaole; Riley J Workman; Zhenmin Hong; Jeffry D Madura; Sanford A Asher
Journal:  J Phys Chem B       Date:  2016-03-18       Impact factor: 2.991

10.  Peptide secondary structure folding reaction coordinate: correlation between uv raman amide III frequency, Psi Ramachandran angle, and hydrogen bonding.

Authors:  Aleksandr V Mikhonin; Sergei V Bykov; Nataliya S Myshakina; Sanford A Asher
Journal:  J Phys Chem B       Date:  2006-02-02       Impact factor: 2.991

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  8 in total

1.  UV Resonance Raman Structural Characterization of an (In)soluble Polyglutamine Peptide.

Authors:  Ryan S Jakubek; Stephen E White; Sanford A Asher
Journal:  J Phys Chem B       Date:  2019-02-19       Impact factor: 2.991

2.  Polyglutamine Solution-State Structural Propensity Is Repeat Length Dependent.

Authors:  Ryan S Jakubek; Riley J Workman; Stephen E White; Sanford A Asher
Journal:  J Phys Chem B       Date:  2019-05-01       Impact factor: 2.991

3.  UV Resonance Raman explores protein structural modification upon fibrillation and ligand interaction.

Authors:  Maria Pachetti; Francesco D'Amico; Lorella Pascolo; Stefania Pucciarelli; Alessandro Gessini; Pietro Parisse; Lisa Vaccari; Claudio Masciovecchio
Journal:  Biophys J       Date:  2021-08-30       Impact factor: 3.699

4.  Strategies and Perspectives for UV Resonance Raman Applicability in Clinical Analyses of Human Sperm RNA.

Authors:  Maria Pachetti; Francesco D'Amico; Luisa Zupin; Stefania Luppi; Monica Martinelli; Sergio Crovella; Giuseppe Ricci; Lorella Pascolo
Journal:  Int J Mol Sci       Date:  2021-12-04       Impact factor: 5.923

Review 5.  Challenges in application of Raman spectroscopy to biology and materials.

Authors:  Nikki Kuhar; Sanchita Sil; Taru Verma; Siva Umapathy
Journal:  RSC Adv       Date:  2018-07-20       Impact factor: 4.036

Review 6.  Applications of Single-Molecule Vibrational Spectroscopic Techniques for the Structural Investigation of Amyloid Oligomers.

Authors:  Katrin Ha Phuong Vu; Gerhard Heinrich Blankenburg; Leonardo Lesser-Rojas; Chia-Fu Chou
Journal:  Molecules       Date:  2022-09-30       Impact factor: 4.927

7.  Analysis of Chemisorbed Tribo-Film for Ceramic-on-Ceramic Hip Joint Prostheses by Raman Spectroscopy.

Authors:  Risha Rufaqua; Martin Vrbka; Dušan Hemzal; Dipankar Choudhury; David Rebenda; Ivan Křupka; Martin Hartl
Journal:  J Funct Biomater       Date:  2021-05-01

8.  Far-Off Resonance: Multiwavelength Raman Spectroscopy Probing Amide Bands of Amyloid-β-(37-42) Peptide.

Authors:  Martynas Talaikis; Simona Strazdaitė; Mantas Žiaunys; Gediminas Niaura
Journal:  Molecules       Date:  2020-08-04       Impact factor: 4.411

  8 in total

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