Proton Nuclear Magnetic Resonance Study of Hirudin: Resonance Assignment and Secondary Structure

G. Marius Clore; Dinesh K. Sukumaran; Axel Preuss; Jutta Zarbock; Angela M. Gronenborn

doi:10.1021/bi00376a001

Proton Nuclear Magnetic Resonance Study of Hirudin: Resonance Assignment and Secondary Structure

G. Marius Clore
, Dinesh K. Sukumaran
, Axel Preuss
, Jutta Zarbock
, Angela M. Gronenborn

Chemistry

Max Planck Institute of Biochemistry

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

38 Scopus citations

Abstract

The_lH NMR spectrum of the 65-residue protein hirudin is assigned in a sequential manner by using a combination of two-dimensional nuclear magnetic resonance techniques to demonstrate through-bond and through-space (<5-A) connectivities. The secondary structure of hirudin is deduced from a qualitative interpretation of the nuclear Overhauser effects involving the backbone NH, C_aH, and C_βH protons. It is shown that hirudin has two β-sheets and no a-helices.

Original language	English
Pages (from-to)	333-338
Number of pages	6
Journal	Biochemistry
Volume	26
Issue number	2
DOIs	https://doi.org/10.1021/bi00376a001
State	Published - 1987

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title = "Proton Nuclear Magnetic Resonance Study of Hirudin: Resonance Assignment and Secondary Structure",

abstract = "ThelH NMR spectrum of the 65-residue protein hirudin is assigned in a sequential manner by using a combination of two-dimensional nuclear magnetic resonance techniques to demonstrate through-bond and through-space (<5-A) connectivities. The secondary structure of hirudin is deduced from a qualitative interpretation of the nuclear Overhauser effects involving the backbone NH, CaH, and CβH protons. It is shown that hirudin has two β-sheets and no a-helices.",

author = "Clore, \{G. Marius\} and Sukumaran, \{Dinesh K.\} and Axel Preuss and Jutta Zarbock and Gronenborn, \{Angela M.\}",

year = "1987",

doi = "10.1021/bi00376a001",

language = "English",

volume = "26",

pages = "333--338",

journal = "Biochemistry",

issn = "0006-2960",

publisher = "American Chemical Society",

number = "2",

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TY - JOUR

T1 - Proton Nuclear Magnetic Resonance Study of Hirudin

T2 - Resonance Assignment and Secondary Structure

AU - Clore, G. Marius

AU - Sukumaran, Dinesh K.

AU - Preuss, Axel

AU - Zarbock, Jutta

AU - Gronenborn, Angela M.

PY - 1987

Y1 - 1987

N2 - ThelH NMR spectrum of the 65-residue protein hirudin is assigned in a sequential manner by using a combination of two-dimensional nuclear magnetic resonance techniques to demonstrate through-bond and through-space (<5-A) connectivities. The secondary structure of hirudin is deduced from a qualitative interpretation of the nuclear Overhauser effects involving the backbone NH, CaH, and CβH protons. It is shown that hirudin has two β-sheets and no a-helices.

AB - ThelH NMR spectrum of the 65-residue protein hirudin is assigned in a sequential manner by using a combination of two-dimensional nuclear magnetic resonance techniques to demonstrate through-bond and through-space (<5-A) connectivities. The secondary structure of hirudin is deduced from a qualitative interpretation of the nuclear Overhauser effects involving the backbone NH, CaH, and CβH protons. It is shown that hirudin has two β-sheets and no a-helices.

UR - https://www.scopus.com/pages/publications/0023094779

U2 - 10.1021/bi00376a001

DO - 10.1021/bi00376a001

M3 - Article

AN - SCOPUS:0023094779

SN - 0006-2960

VL - 26

SP - 333

EP - 338

JO - Biochemistry

JF - Biochemistry

IS - 2

ER -

Proton Nuclear Magnetic Resonance Study of Hirudin: Resonance Assignment and Secondary Structure

Abstract

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