A Study of Phenylalanine Side Chain Dynamics in Surface-Adsorbed Peptides Using Solid State Deuterium NMR and Rotamer Library Statistics.
J Am Chem Soc. 2014 Jul 23;
Authors: Li K, Emani PS, Ash J, Groves M, Drobny GP
Abstract
Extracellular matrix proteins adsorbed onto mineral surfaces exist in a unique environment where the structure and dynamics of the protein can be altered profoundly. To further elucidate how the mineral surface impacts molecular properties, we perform a comparative study of the dynamics of non-polar side chains within the mineral-recognition domain of the biomineralization protein salivary statherin adsorbed onto its native hydroxyapatite (HAP) mineral surface versus the dynamics displayed by the native protein in the hydrated solid state. Specifically, the dynamics of phenylalanine side chains (viz. F7 and F14) located in the surface-adsorbed fifteen amino acid HAP-recognition fragment (SN-15) are studied using deuterium magic angle spinning ((2)H MAS) line shape and spin lattice relaxation measurements. (2)H NMR MAS spectra and T1 relaxation times obtained from the deuterated phenylalanine side chains in free and HAP-adsorbed SN-15 are fitted to models where the side chains are assumed to exchange between rotameric states, and where the exchange rates and a priori rotameric state populations are varied iteratively. In condensed proteins, phenylalanine side chain dynamics are dominated by 180° flips of the phenyl ring, i.e. the "? flip". However, for both F7 and F14 the number of exchanging side chain rotameric states increases in the HAP-bound complex relative to the unbound solid sample indicating that increased dynamic freedom accompanies introduction of the protein into the biofilm state. The observed rotameric exchange dynamics in the HAP-bound complex are on the order of 5-6×10(6) s(-1), as determined from the deuterium MAS lineshapes. The dynamics in the HAP-bound complex are also shown to have some solution-like behavioral characteristics, with some interesting deviations from rotameric library statistics.
PMID: 25054469 [PubMed - as supplied by publisher]
Proton Clouds to Measure Long-Range Contacts between Nonexchangeable Side Chain Protons in Solid-State NMR
Proton Clouds to Measure Long-Range Contacts between Nonexchangeable Side Chain Protons in Solid-State NMR
Tessa Sinnige, Mark Danie?ls, Marc Baldus and Markus Weingarth
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja412870m/aop/images/medium/ja-2013-12870m_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/ja412870m
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/0gtd6wPcuVY
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Solid-State NMR Measurements of Asymmetric Dipolar Couplings Provide Insight into Protein Side-Chain Motion.
Solid-State NMR Measurements of Asymmetric Dipolar Couplings Provide Insight into Protein Side-Chain Motion.
Solid-State NMR Measurements of Asymmetric Dipolar Couplings Provide Insight into Protein Side-Chain Motion.
Angew Chem Int Ed Engl. 2011 Sep 16;
Authors: Schanda P, Huber M, Boisbouvier J, Meier BH, Ernst M
PMID: 21928443
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Deuterium Magic Angle Spinning NMR Used to Study the Dynamics of Peptides Adsorbed onto Polystyrene and Functionalized Polystyrene Surfaces.
Deuterium Magic Angle Spinning NMR Used to Study the Dynamics of Peptides Adsorbed onto Polystyrene and Functionalized Polystyrene Surfaces.
Deuterium Magic Angle Spinning NMR Used to Study the Dynamics of Peptides Adsorbed onto Polystyrene and Functionalized Polystyrene Surfaces.
J Phys Chem B. 2011 Jun 8;
Authors: Breen NF, Li K, Olsen GL, Drobny GP
LK?14 is a 14 amino acid peptide which displays a periodic alternation of leucine and lysine amino acids. This "hydrophobic periodicity" has been found to result in an ?-helical secondary structure...
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06-10-2011 11:52 AM
[NMR paper] Probing side-chain dynamics in high molecular weight proteins by deuterium NMR spin r
Probing side-chain dynamics in high molecular weight proteins by deuterium NMR spin relaxation: an application to an 82-kDa enzyme.
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J Am Chem Soc. 2005 Jun 8;127(22):8214-25
Authors: Tugarinov V, Ollerenshaw JE, Kay LE
New NMR experiments for the measurement of side-chain dynamics in high molecular weight ( approximately 100 kDa) proteins are presented. The experiments quantify (2)H spin...
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11-25-2010 08:21 PM
[NMR paper] Side chain dynamics in unfolded protein states: an NMR based 2H spin relaxation study
Side chain dynamics in unfolded protein states: an NMR based 2H spin relaxation study of delta131delta.
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J Am Chem Soc. 2003 Feb 19;125(7):1748-58
Authors: Choy WY, Shortle D, Kay LE
NMR relaxation data on disordered proteins can provide insight into both structural and dynamic properties of these molecules. Because of chemical shift degeneracy in correlation spectra, detailed site-specific analyses of side chain dynamics...
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11-24-2010 09:01 PM
[NMR paper] Main chain and side chain dynamics of a heme protein: 15N and 2H NMR relaxation studi
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Biochemistry. 2001 Jun 5;40(22):6559-69
Authors: Flynn PF, Bieber Urbauer RJ, Zhang H, Lee AL, Wand AJ
A detailed characterization of the main chain and side chain dynamics in R. capsulatus ferrocytochrome c(2) derived from (2)H NMR relaxation of methyl group resonances is...
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11-19-2010 08:32 PM
[NMR paper] Side chain accessibility and dynamics in the molten globule state of alpha-lactalbumi
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Biochemistry. 2000 Jan 18;39(2):372-80
Authors: Bai P, Luo L, Peng Z
The molten globule state of alpha-lactalbumin (alpha-LA) has been considered a prototype of partially folded proteins. Despite the importance of molten globules in understanding the mechanisms of protein folding and its relevance to some biological...
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[NMR paper] A study of protein side-chain dynamics from new 2H auto-correlation and 13C cross-cor
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J Mol Biol. 1998 Mar 13;276(5):939-54
Authors: Yang D, Mittermaier A, Mok YK, Kay LE
Two new NMR experiments are presented for measuring side-chain dynamics in proteins. The first method, requiring 15N, 13C,...