A critical evaluation of the predicted and X-ray structures of α-Lactalbumin

K. Ravi Acharya, David I. Stuart, David C. Phillips, Harold A. Scheraga

Research output: Contribution to journalArticle

Abstract

The rapidly increasing availability of protein amino-acid sequences, many of which have been determined from the corresponding gene sequences, has intensified interest in the prediction of related protein structures when the three-dimensional structure of another member of the family is known. The study of bovine α-Lactalbumin provides a classic example in which the three-dimensional structure was predicted, first by Browne et al. (1969) and later by Warme et al. (1974), from the three-dimensional structure of hen-egg-white lysozyme (Blake et al., 1965), taking into account the striking relationship between the amino acid sequences of the two proteins. A comprehensive comparison of these models with the structure of baboon α-Lactalbumin derived from X-ray crystallography (Acharya et al., 1989) is presented. The models mostly compare well with the experimentally determined structure except in the flexible C-terminal region of the molecule (rms deviation on Cα of residues 1-95, 1.1 Å).

Original languageEnglish
Pages (from-to)549-563
Number of pages15
JournalJournal of Protein Chemistry
Volume9
Issue number5
DOIs
Publication statusPublished - 1 Oct 1990

Keywords

  • α-Lactalbumin
  • computer modeling
  • lysozyme
  • X-ray crystallography

ASJC Scopus subject areas

  • Biochemistry

Cite this

A critical evaluation of the predicted and X-ray structures of α-Lactalbumin. / Acharya, K. Ravi; Stuart, David I.; Phillips, David C.; Scheraga, Harold A.

In: Journal of Protein Chemistry, Vol. 9, No. 5, 01.10.1990, p. 549-563.

Research output: Contribution to journalArticle

Acharya, K. Ravi ; Stuart, David I. ; Phillips, David C. ; Scheraga, Harold A. / A critical evaluation of the predicted and X-ray structures of α-Lactalbumin. In: Journal of Protein Chemistry. 1990 ; Vol. 9, No. 5. pp. 549-563.
@article{de90b333593b44d0968f364744a79d38,
title = "A critical evaluation of the predicted and X-ray structures of α-Lactalbumin",
abstract = "The rapidly increasing availability of protein amino-acid sequences, many of which have been determined from the corresponding gene sequences, has intensified interest in the prediction of related protein structures when the three-dimensional structure of another member of the family is known. The study of bovine α-Lactalbumin provides a classic example in which the three-dimensional structure was predicted, first by Browne et al. (1969) and later by Warme et al. (1974), from the three-dimensional structure of hen-egg-white lysozyme (Blake et al., 1965), taking into account the striking relationship between the amino acid sequences of the two proteins. A comprehensive comparison of these models with the structure of baboon α-Lactalbumin derived from X-ray crystallography (Acharya et al., 1989) is presented. The models mostly compare well with the experimentally determined structure except in the flexible C-terminal region of the molecule (rms deviation on Cα of residues 1-95, 1.1 {\AA}).",
keywords = "α-Lactalbumin, computer modeling, lysozyme, X-ray crystallography",
author = "Acharya, {K. Ravi} and Stuart, {David I.} and Phillips, {David C.} and Scheraga, {Harold A.}",
year = "1990",
month = "10",
day = "1",
doi = "10.1007/BF01025008",
language = "English",
volume = "9",
pages = "549--563",
journal = "Journal of Protein Chemistry",
issn = "0277-8033",
number = "5",

}

TY - JOUR

T1 - A critical evaluation of the predicted and X-ray structures of α-Lactalbumin

AU - Acharya, K. Ravi

AU - Stuart, David I.

AU - Phillips, David C.

AU - Scheraga, Harold A.

PY - 1990/10/1

Y1 - 1990/10/1

N2 - The rapidly increasing availability of protein amino-acid sequences, many of which have been determined from the corresponding gene sequences, has intensified interest in the prediction of related protein structures when the three-dimensional structure of another member of the family is known. The study of bovine α-Lactalbumin provides a classic example in which the three-dimensional structure was predicted, first by Browne et al. (1969) and later by Warme et al. (1974), from the three-dimensional structure of hen-egg-white lysozyme (Blake et al., 1965), taking into account the striking relationship between the amino acid sequences of the two proteins. A comprehensive comparison of these models with the structure of baboon α-Lactalbumin derived from X-ray crystallography (Acharya et al., 1989) is presented. The models mostly compare well with the experimentally determined structure except in the flexible C-terminal region of the molecule (rms deviation on Cα of residues 1-95, 1.1 Å).

AB - The rapidly increasing availability of protein amino-acid sequences, many of which have been determined from the corresponding gene sequences, has intensified interest in the prediction of related protein structures when the three-dimensional structure of another member of the family is known. The study of bovine α-Lactalbumin provides a classic example in which the three-dimensional structure was predicted, first by Browne et al. (1969) and later by Warme et al. (1974), from the three-dimensional structure of hen-egg-white lysozyme (Blake et al., 1965), taking into account the striking relationship between the amino acid sequences of the two proteins. A comprehensive comparison of these models with the structure of baboon α-Lactalbumin derived from X-ray crystallography (Acharya et al., 1989) is presented. The models mostly compare well with the experimentally determined structure except in the flexible C-terminal region of the molecule (rms deviation on Cα of residues 1-95, 1.1 Å).

KW - α-Lactalbumin

KW - computer modeling

KW - lysozyme

KW - X-ray crystallography

UR - http://www.scopus.com/inward/record.url?scp=0025690072&partnerID=8YFLogxK

U2 - 10.1007/BF01025008

DO - 10.1007/BF01025008

M3 - Article

VL - 9

SP - 549

EP - 563

JO - Journal of Protein Chemistry

JF - Journal of Protein Chemistry

SN - 0277-8033

IS - 5

ER -