De novo determination of peptide structure with solid-state magic-angle spinning NMR spectroscopy

Chad M. Rienstra; Lisa Tucker-Kellogg; Christopher P. Jaroniec; Morten Hohwy; Bernd Reif; Michael T. McMahon; Bruce Tidor; Tomás Lozano-Pérez; Robert G. Griffin

doi:10.1073/pnas.152346599

De novo determination of peptide structure with solid-state magic-angle spinning NMR spectroscopy

Chad M. Rienstra, Lisa Tucker-Kellogg, Christopher P. Jaroniec, Morten Hohwy, Bernd Reif, Michael T. McMahon, Bruce Tidor, Tomás Lozano-Pérez, Robert G. Griffin

Francis Bitter Magnet Laboratory

Research output: Contribution to journal › Article › peer-review

244 Scopus citations

Abstract

The three-dimensional structure of the chemotactic peptide N-formyl-L-Met-L-Leu-L-Phe-OH was determined by using solid-state NMR (SSNMR). The set of SSNMR data consisted of 16 ¹³C-¹⁵N distances and 18 torsion angle constraints (on 10 angles), recorded from uniformly ¹³C, ¹⁵N- and ¹⁵N-labeled samples. The peptide's structure was calculated by means of simulated annealing and a newly developed protocol that ensures that all of conformational space, consistent with the structural constraints, is searched completely. The result is a high-quality structure of a molecule that has thus far not been amenable to single-crystal diffraction studies. The extensions of the SSNMR techniques and computational methods to larger systems appear promising.

Original language	English
Pages (from-to)	10260-10265
Number of pages	6
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	99
Issue number	16
DOIs	https://doi.org/10.1073/pnas.152346599
State	Published - Aug 2002
Externally published	Yes

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Rienstra, C. M., Tucker-Kellogg, L., Jaroniec, C. P., Hohwy, M., Reif, B., McMahon, M. T., Tidor, B., Lozano-Pérez, T., & Griffin, R. G. (2002). De novo determination of peptide structure with solid-state magic-angle spinning NMR spectroscopy. Proceedings of the National Academy of Sciences of the United States of America, 99(16), 10260-10265. https://doi.org/10.1073/pnas.152346599

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title = "De novo determination of peptide structure with solid-state magic-angle spinning NMR spectroscopy",

abstract = "The three-dimensional structure of the chemotactic peptide N-formyl-L-Met-L-Leu-L-Phe-OH was determined by using solid-state NMR (SSNMR). The set of SSNMR data consisted of 16 13C-15N distances and 18 torsion angle constraints (on 10 angles), recorded from uniformly 13C, 15N- and 15N-labeled samples. The peptide's structure was calculated by means of simulated annealing and a newly developed protocol that ensures that all of conformational space, consistent with the structural constraints, is searched completely. The result is a high-quality structure of a molecule that has thus far not been amenable to single-crystal diffraction studies. The extensions of the SSNMR techniques and computational methods to larger systems appear promising.",

author = "Rienstra, {Chad M.} and Lisa Tucker-Kellogg and Jaroniec, {Christopher P.} and Morten Hohwy and Bernd Reif and McMahon, {Michael T.} and Bruce Tidor and Tom{\'a}s Lozano-P{\'e}rez and Griffin, {Robert G.}",

year = "2002",

month = aug,

doi = "10.1073/pnas.152346599",

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volume = "99",

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Rienstra, CM, Tucker-Kellogg, L, Jaroniec, CP, Hohwy, M, Reif, B, McMahon, MT, Tidor, B, Lozano-Pérez, T & Griffin, RG 2002, 'De novo determination of peptide structure with solid-state magic-angle spinning NMR spectroscopy', Proceedings of the National Academy of Sciences of the United States of America, vol. 99, no. 16, pp. 10260-10265. https://doi.org/10.1073/pnas.152346599

TY - JOUR

T1 - De novo determination of peptide structure with solid-state magic-angle spinning NMR spectroscopy

AU - Rienstra, Chad M.

AU - Tucker-Kellogg, Lisa

AU - Jaroniec, Christopher P.

AU - Hohwy, Morten

AU - Reif, Bernd

AU - McMahon, Michael T.

AU - Tidor, Bruce

AU - Lozano-Pérez, Tomás

AU - Griffin, Robert G.

PY - 2002/8

Y1 - 2002/8

N2 - The three-dimensional structure of the chemotactic peptide N-formyl-L-Met-L-Leu-L-Phe-OH was determined by using solid-state NMR (SSNMR). The set of SSNMR data consisted of 16 13C-15N distances and 18 torsion angle constraints (on 10 angles), recorded from uniformly 13C, 15N- and 15N-labeled samples. The peptide's structure was calculated by means of simulated annealing and a newly developed protocol that ensures that all of conformational space, consistent with the structural constraints, is searched completely. The result is a high-quality structure of a molecule that has thus far not been amenable to single-crystal diffraction studies. The extensions of the SSNMR techniques and computational methods to larger systems appear promising.

AB - The three-dimensional structure of the chemotactic peptide N-formyl-L-Met-L-Leu-L-Phe-OH was determined by using solid-state NMR (SSNMR). The set of SSNMR data consisted of 16 13C-15N distances and 18 torsion angle constraints (on 10 angles), recorded from uniformly 13C, 15N- and 15N-labeled samples. The peptide's structure was calculated by means of simulated annealing and a newly developed protocol that ensures that all of conformational space, consistent with the structural constraints, is searched completely. The result is a high-quality structure of a molecule that has thus far not been amenable to single-crystal diffraction studies. The extensions of the SSNMR techniques and computational methods to larger systems appear promising.

UR - http://www.scopus.com/inward/record.url?scp=0036678408&partnerID=8YFLogxK

U2 - 10.1073/pnas.152346599

DO - 10.1073/pnas.152346599

M3 - Article

C2 - 12149447

AN - SCOPUS:0036678408

SN - 0027-8424

VL - 99

SP - 10260

EP - 10265

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

IS - 16

ER -

De novo determination of peptide structure with solid-state magic-angle spinning NMR spectroscopy

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