About: New X-Ray Evidence on the Configuration of Polypeptide Chains: Polypeptide Chains in Poly-γ-benzyl-L-glutamate, Keratin and Hæmoglobin

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About: New X-Ray Evidence on the Configuration of Polypeptide Chains: Polypeptide Chains in Poly-γ-benzyl-L-glutamate, Keratin and Hæmoglobin Goto Sponge NotDistinct Permalink

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scientific article published in Nature

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rdf:type	Item
description	artículu científicu (ast) wetenschappelijk artikel (nl) article publié dans la revue scientifique Nature (fr) নেচারে প্রকাশিত বৈজ্ঞানিক প্রবন্ধ (bn) scientific article published in Nature (en) im Juni 1951 veröffentlichter wissenschaftlicher Artikel (de) наукова стаття, опублікована в Nature в червні 1951 (uk)
publication date	wds:Q56688811-F88225B5-6B3F-4D7C-AFCE-B4696C4A4E43
publication date	1951-06-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q56688811-C7F6277A-1154-4B55-96B4-3B9EAF039357
language of work or name	English
exact match	wds:Q56688811-62D6043D-6F83-4EC1-8490-7EDD33ABAF45
exact match	https://scigraph.springernature.com/pub.10.1038/1671053a0
cites work	wds:Q56688811-017D8392-1ED1-4A1C-9F64-5F82D3FF8DAC wds:Q56688811-0826F342-E112-4ABD-9DF5-0DD9D67E62EF wds:Q56688811-0E7890EB-92C7-46C9-B2E0-078AA5F6AB21 wds:Q56688811-1FEE5623-51ED-4B11-BA58-1CD6CF831061 wds:Q56688811-3DBE6FC5-FC2D-4742-B89C-F4C5A0A5F879 wds:Q56688811-4DA2C466-651C-417B-88A4-97431B61F425 wds:Q56688811-697A1D8D-5146-4808-897B-35F1E2F9DFD0 wds:Q56688811-984A03FF-0E24-46CD-B3D4-F21F6272276D wds:Q56688811-A501ABFD-27B0-47AB-AA87-F51574237C4F wds:Q56688811-EC331FC5-472E-4EC3-A666-08DAA9EC8BDD wds:Q56688811-F6AF04D4-54B2-4C55-ADC5-92DFFF8CE2CA
cites work	The structure of proteins; two hydrogen-bonded helical configurations of the polypeptide chain The structure of synthetic polypeptides STRUCTURE OF α-KERATIN The structure of feather rachis keratin The structure of hair, muscle, and related proteins New evidence on the structure of some proteins from measurements with polarized infra-red radiation. Polypeptide Chain Configurations in Crystalline Proteins The Structure of Fibrous Proteins Nature of the Intramolecular Fold in Alpha-Keratin and Alpha-Myosin The Structure of Synthetic Polypeptides. I. X-Ray Investigation An X-ray study of horse methemoglobin.
author name string	wds:Q56688811-27927B5D-013F-4909-BE2A-E71227BC35E0
author name string	M F PERUTZ
rdfs:label	New X-Ray Evidence on the Configuration of Polypeptide Chains: Polypeptide Chains in Poly-γ-benzyl-L-glutamate, Keratin and Hæmoglobin (en) New X-Ray Evidence on the Configuration of Polypeptide Chains: Polypeptide Chains in Poly-γ-benzyl-L-glutamate, Keratin and Hæmoglobin (nl)
skos:prefLabel	New X-Ray Evidence on the Configuration of Polypeptide Chains: Polypeptide Chains in Poly-γ-benzyl-L-glutamate, Keratin and Hæmoglobin (en) New X-Ray Evidence on the Configuration of Polypeptide Chains: Polypeptide Chains in Poly-γ-benzyl-L-glutamate, Keratin and Hæmoglobin (nl)
name	New X-Ray Evidence on the Configuration of Polypeptide Chains: Polypeptide Chains in Poly-γ-benzyl-L-glutamate, Keratin and Hæmoglobin (en) New X-Ray Evidence on the Configuration of Polypeptide Chains: Polypeptide Chains in Poly-γ-benzyl-L-glutamate, Keratin and Hæmoglobin (nl)
title	wds:Q56688811-577599C5-4A44-4919-8966-5E1DAFB79BEC
title	New x-ray evidence on the configuration of polypeptide chains (en)
page(s)	wds:Q56688811-1F1B98F1-A2C6-4214-9D96-E5E0CDDBA093
page(s)	1053-1054
instance of	wds:Q56688811-774F098D-6777-494B-874D-4574455E8116
instance of	scholarly article
PubMed ID	wds:Q56688811-60534391-596B-4574-91C2-06076D3DB164
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/14843172
PubMed ID	14843172
published in	wds:Q56688811-AF91CF7F-C8E7-4FCA-B89A-A459723A2E4A
published in	Nature
issue	wds:Q56688811-6BEF0190-56D2-482E-A9D1-3C52E0C2AD72
volume	wds:Q56688811-7292EC15-BEBF-4C1A-896B-8E86AA1AE44B
issue	4261
volume	167
DOI	wds:Q56688811-84826C69-432E-474C-930C-76B6FF41F1F8
DOI	http://dx.doi.org/10.1038/1671053A0
DOI	10.1038/1671053A0
Dimensions Publication ID	wds:Q56688811-E0936501-EF9E-4797-8176-3EA16B57ABB9
Dimensions Publication ID	1021187696
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q56688811
is cites work of	Structure of myoglobin: A three-dimensional Fourier synthesis at 2 A. resolution A fresh look at the Ramachandran plot and the occurrence of standard structures in proteins High-resolution crystal structures of protein helices reconciled with three-centered hydrogen bonds and multipole electrostatics Optical rotation and the conformation of polypeptides and proteins Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins Ionization Behaviour of Native Apolipoproteins and of Their Complexes with Lecithin. 1. Calorimetric and Potentiometric Titration of the Native ApoA-I Protein and of the ApoA-I Protein - Dimyristoyl Lecithin Complex Is alpha-keratin a coiled coil? The anatomy and taxonomy of protein structure O-Linked glycopeptides retain helicity in water Conformation of Polypeptides and Proteins Stability and design of alpha-helical peptides. Configurations of Polypeptide Chains With Favored Orientations Around Single Bonds: Two New Pleated Sheets Crystal structure of sickle-cell deoxyhemoglobin at 5 A resolution. Compound Helical Configurations of Polypeptide Chains: Structure of Proteins of the α-Keratin Type The sulfur chemistry of proteins Side-chain entropy opposes alpha-helix formation but rationalizes experimentally determined helix-forming propensities Identification of local variations within secondary structures of proteins. Recent advances in helix-coil theory. Streptococcal M protein: molecular design and biological behavior. A method for structural analysis of alpha-helices of membrane proteins. Stabilization of alpha-helical structures in short peptides via end capping A thermodynamic model for gelation of sickle-cell hemoglobin Isolation and characterization of the cell-associated region of group A streptococcal M6 protein Determination of molecular order in supported lipid membranes by internal reflection Fourier transform infrared spectroscopy Evaluation of the structural quality of modeled proteins by using globularity criteria Interactions between hydrophobic side chains within alpha-helices Protein structure in relation to function and biosynthesis. Glatiramer acetate in treatment of multiple sclerosis: a toolbox of random co-polymers for targeting inflammatory mechanisms of both the innate and adaptive immune system? Evidence for the Pauling–Corey α-Helix in Synthetic Polypeptides Structure of Synthetic Polypeptides Solvent-induced distortions and the curvature of alpha-helices Conformation changes in the nonionizable water-soluble synthetic polypeptide poly-N5-(3-hydroxypropyl) -L-glutamine Conformation of poly(γ-glutamic acid) in aqueous solution THE HEMOGLOBINS Helicoidal self-ordering of cellulose microfibrils in aqueous suspension

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