Crystal and molecular structure of l‐valyl‐l‐lysine hydrochloride

Hemant P. Yennawar, S. NATARAJAN, MA VISWAMITRA

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

l‐Valyl‐l‐lysine hydrochloride, C11N3O3H23 HCl, crystallizes in the monoclinic space group P2, with a = 5.438(5), b = 14.188(5), c = 9.521(5) Å, β= 95.38(2)° and Z = 2. The crystal structure, solved by direct methods, refined to R = 0.036, using full matrix least‐squares method. The peptide exists in a zwitterionic form, with the N atom of the lysine side‐chain protonated. The two γ‐carbons of the valine side‐chain have positional disorder, giving rise to two conformations, χ111= ‐67.3 and 65.9°, one of which (65.9°) is sterically less favourable and has been found to be less popular amongst residues branching at β‐C. The lysine side‐chain has the geometry of g tgt, not seen in crystal structures of the dipeptides reported so far. Interestingly, χ32 (63.6°) of lysine side‐chain has a gauche+ conformation unlike in most of the other structures, where it is trans. The neighbouring peptide molecules are hydrogen bonded in a head‐to‐tail fashion, a rather uncommon interaction in lysine peptide structures. The structure shows considerable similarity with that of l‐Lys‐l‐Val HO in conformational angles and H‐bond interactions [4].

Original languageEnglish (US)
Pages (from-to)569-573
Number of pages5
JournalInternational Journal of Peptide and Protein Research
Volume38
Issue number6
DOIs
StatePublished - Jan 1 1991

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Molecular Structure
Molecular structure
Lysine
Crystal structure
Peptides
Conformations
Dipeptides
Valine
Hydrogen
Carbon
Atoms
Molecules
Geometry

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

@article{93974202190a42249e0085d99b80de65,
title = "Crystal and molecular structure of l‐valyl‐l‐lysine hydrochloride",
abstract = "l‐Valyl‐l‐lysine hydrochloride, C11N3O3H23 HCl, crystallizes in the monoclinic space group P2, with a = 5.438(5), b = 14.188(5), c = 9.521(5) {\AA}, β= 95.38(2)° and Z = 2. The crystal structure, solved by direct methods, refined to R = 0.036, using full matrix least‐squares method. The peptide exists in a zwitterionic form, with the N atom of the lysine side‐chain protonated. The two γ‐carbons of the valine side‐chain have positional disorder, giving rise to two conformations, χ111= ‐67.3 and 65.9°, one of which (65.9°) is sterically less favourable and has been found to be less popular amongst residues branching at β‐C. The lysine side‐chain has the geometry of g− tgt, not seen in crystal structures of the dipeptides reported so far. Interestingly, χ32 (63.6°) of lysine side‐chain has a gauche+ conformation unlike in most of the other structures, where it is trans. The neighbouring peptide molecules are hydrogen bonded in a head‐to‐tail fashion, a rather uncommon interaction in lysine peptide structures. The structure shows considerable similarity with that of l‐Lys‐l‐Val HO in conformational angles and H‐bond interactions [4].",
author = "Yennawar, {Hemant P.} and S. NATARAJAN and MA VISWAMITRA",
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Crystal and molecular structure of l‐valyl‐l‐lysine hydrochloride. / Yennawar, Hemant P.; NATARAJAN, S.; VISWAMITRA, MA.

In: International Journal of Peptide and Protein Research, Vol. 38, No. 6, 01.01.1991, p. 569-573.

Research output: Contribution to journalArticle

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T1 - Crystal and molecular structure of l‐valyl‐l‐lysine hydrochloride

AU - Yennawar, Hemant P.

AU - NATARAJAN, S.

AU - VISWAMITRA, MA

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Y1 - 1991/1/1

N2 - l‐Valyl‐l‐lysine hydrochloride, C11N3O3H23 HCl, crystallizes in the monoclinic space group P2, with a = 5.438(5), b = 14.188(5), c = 9.521(5) Å, β= 95.38(2)° and Z = 2. The crystal structure, solved by direct methods, refined to R = 0.036, using full matrix least‐squares method. The peptide exists in a zwitterionic form, with the N atom of the lysine side‐chain protonated. The two γ‐carbons of the valine side‐chain have positional disorder, giving rise to two conformations, χ111= ‐67.3 and 65.9°, one of which (65.9°) is sterically less favourable and has been found to be less popular amongst residues branching at β‐C. The lysine side‐chain has the geometry of g− tgt, not seen in crystal structures of the dipeptides reported so far. Interestingly, χ32 (63.6°) of lysine side‐chain has a gauche+ conformation unlike in most of the other structures, where it is trans. The neighbouring peptide molecules are hydrogen bonded in a head‐to‐tail fashion, a rather uncommon interaction in lysine peptide structures. The structure shows considerable similarity with that of l‐Lys‐l‐Val HO in conformational angles and H‐bond interactions [4].

AB - l‐Valyl‐l‐lysine hydrochloride, C11N3O3H23 HCl, crystallizes in the monoclinic space group P2, with a = 5.438(5), b = 14.188(5), c = 9.521(5) Å, β= 95.38(2)° and Z = 2. The crystal structure, solved by direct methods, refined to R = 0.036, using full matrix least‐squares method. The peptide exists in a zwitterionic form, with the N atom of the lysine side‐chain protonated. The two γ‐carbons of the valine side‐chain have positional disorder, giving rise to two conformations, χ111= ‐67.3 and 65.9°, one of which (65.9°) is sterically less favourable and has been found to be less popular amongst residues branching at β‐C. The lysine side‐chain has the geometry of g− tgt, not seen in crystal structures of the dipeptides reported so far. Interestingly, χ32 (63.6°) of lysine side‐chain has a gauche+ conformation unlike in most of the other structures, where it is trans. The neighbouring peptide molecules are hydrogen bonded in a head‐to‐tail fashion, a rather uncommon interaction in lysine peptide structures. The structure shows considerable similarity with that of l‐Lys‐l‐Val HO in conformational angles and H‐bond interactions [4].

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