scispace - formally typeset
Search or ask a question
Book•

Atlas of protein sequence and structure

About: The article was published on 1965-01-01 and is currently open access. It has received 6855 citations till now. The article focuses on the topics: Protein primary structure & Peptide sequence.

Content maybe subject to copyright    Report


ATLAS
of
PROTEIN
SEQUENCE
and
STRUCTURE
1965 zyxwvutsrqponmlkjihgfedcbaZYXWVUTSRQPONMLKJIHGFEDCBA
Margaret
0.
Dayhoff
Richard
V.
Eck
Marie
A.
Chang
Minnie
R.
Sochard
NATIONAL
BIOMEDICAL
RESEARCH
FOUNDATION
8600
16~~
STREET zyxwvutsrqponmlkjihgfedcbaZYXWVUTSRQPONMLKJIHGFEDCBA
Silw
Spring,
Ma
yhnd

ATLAS
OF
PROTEIN SEQUENCE AND STRUCTURE zyxwvutsrqponmlkjihgfedcbaZYXWVUTSRQPONMLKJIHGFEDCBA
1965
Library
of
Congress Card Catalogue Number
65-29342 zyxwvutsrqponmlkjihgfedcbaZYXWVUTSRQPONMLKJIHGFEDCBA
@
Copyright
1965
by
The National Biomedical Research Foundation
Extra copies may be purchased from:
The National Biomedical Research Foundation
8600 16th Street, Silver Spring, Maryland

DEDICATION zyxwvutsrqponmlkjihgfedcbaZYXWVUTSRQPONMLKJIHGFEDCBA
To zyxwvutsrqponmlkjihgfedcbaZYXWVUTSRQPONMLKJIHGFEDCBA
all
the investigators who have developed the techniques
necessary for the grand accomplishments represented by this tabu-
lation, and to
all
those who have spent zyxwvutsrqponmlkjihgfedcbaZYXWVUTSRQPONMLKJIHGFEDCBA
so
much tedious effort in
their application.
We
would gratefully appreciate receiving suggestions, correc-
tions, new data (even
if
fragmentary or provisional), and
refer-
ences to any data omitted from this volume.
M. zyxwvutsrqponmlkjihgfedcbaZYXWVUTSRQPONMLKJIHGFEDCBA
0.
D.
R.
V.
E.
M.
A. zyxwvutsrqponmlkjihgfedcbaZYXWVUTSRQPONMLKJIHGFEDCBA
C.
M.
R.
S.

.001 zyxwvutsrqponmlkjihgfedcbaZYXWVUTSRQPONMLKJIHGFEDCBA
PREFACE
This
Atlas
voluminously illustrates the triumph of experimental technique over
the secretiveness of nature. Perhaps nowhere has the power of the scientific method
been more brilliantly demonstrated than in the development of procedures for the
study of the chemistry of life.
As
recently
as
twenty years ago,
it
was customary for
biologists
to
have
a
hopeless attitude about biochemistry. Some details might be
elicited, perhaps, but living things were thought to be
so
very complex and intricate
that
there surely was no hope of fully "understanding" them in
all
their chemical de-
tail.
Who,
if
he really comprehended the difficulty of the problem, would dare
to
think
'of man's ever knowing the detailed structure of
a
protein, for example, much
less
be
able
to synthesize
it?
Who
would ever understand the mechanism of
an
enzyme
as
clearly
as
a
chemist understands the details of an inorganic reaction? How could we
ever hope to know the atomic details of
a
protein crystal zyxwvutsrqponmlkjihgfedcbaZYXWVUTSRQPONMLKJIHGFEDCBA
?
Today some of these ambitions have already been attained, and the others no
longer seem out of reach.
We
now rationally hope to be able to discover and under-
stand the finest chemical details of living processes.
These accomplishments and
hopes have been made possible by the combined
effect
of several new approaches.
Techniques which permit the separation of chemically similar compounds have
been developed for microgram samples.
Among these
are
ion-exchange columns,
paper chromatography, electrophoresis, and counter-current distribution. Radio-
active
tracer
techniques and other micro-quantitative analytical procedures, often de-
pendent on electronics and automation, have aided the 'analyses. X-ray crystallography,
starting with
the
art
of protein crystal production and ending with the processing of
great numbers of experimental observations in the high-speed computer, has permitted
a
glimpse of three-dimensional structure.
Confidence in our understanding of experimental procedures and relationships
among proteins
has
grown
so
great that sequences of amino acids
are
inferred from
those found in homologous proteins. This technique requires only
a
small proportion
of
the analytical work needed to sequence
a
protein with no known relatives.
The ef-
fectiveness of laboratory effort
is
thus magnified.
Some
of
the insights which have been developed cannot be attributed to any partic-
ular
worker
or
school. Perhaps the greatest
of
these insights
is
that nature always
uses "building blocks."
A
living cell
is
extremely complex and almost unimaginably
intricate in detail.
But
it
consists of
a
limited, understandable number of types of
processes, reduplicated with variations.
To understand the cell,
we
must have
a
few
examples of each
type
of process, from which we can see the overall principles. For
understanding,
we
need not work out the details of
all
the variations on these princi-
ples, although we may eventually choose to
do
so
for medical
or
other practical
rea-
sons. Similarly, the analysis of such large, complex chemical molecules
as
proteins
has been made possible by the recognition of their essential modularity, their building-
block nature. Proteins
are
precise chemical structures built from
regular
subunits,

Citations
More filters
Journal Article•DOI•
TL;DR: A new approach to rapid sequence comparison, basic local alignment search tool (BLAST), directly approximates alignments that optimize a measure of local similarity, the maximal segment pair (MSP) score.

88,255 citations


Cites background from "Atlas of protein sequence and struc..."

  • ...…• combined with phylogenetic studies o can determine orthologous and paralogous relationships Local Alignment • uses a subset of a sequence and attempts to align it to subset of other sequences • computationally less expensive than other methods Local Alignment Example • a small seed is uncovered...

    [...]

  • ...TAT ||| AAGCGAATAATATATTTATACTCAGATTATTGCGCG • And now the extended alignment: TATATATTAGTA ||||||||| || AAGCGAATAATATATTTATACTCAGATTATTGCGCG...

    [...]

Journal Article•DOI•
TL;DR: A new criterion for triggering the extension of word hits, combined with a new heuristic for generating gapped alignments, yields a gapped BLAST program that runs at approximately three times the speed of the original.
Abstract: The BLAST programs are widely used tools for searching protein and DNA databases for sequence similarities. For protein comparisons, a variety of definitional, algorithmic and statistical refinements described here permits the execution time of the BLAST programs to be decreased substantially while enhancing their sensitivity to weak similarities. A new criterion for triggering the extension of word hits, combined with a new heuristic for generating gapped alignments, yields a gapped BLAST program that runs at approximately three times the speed of the original. In addition, a method is introduced for automatically combining statistically significant alignments produced by BLAST into a position-specific score matrix, and searching the database using this matrix. The resulting Position-Specific Iterated BLAST (PSIBLAST) program runs at approximately the same speed per iteration as gapped BLAST, but in many cases is much more sensitive to weak but biologically relevant sequence similarities. PSI-BLAST is used to uncover several new and interesting members of the BRCT superfamily.

70,111 citations

Journal Article•DOI•
TL;DR: The sensitivity of the commonly used progressive multiple sequence alignment method has been greatly improved and modifications are incorporated into a new program, CLUSTAL W, which is freely available.
Abstract: The sensitivity of the commonly used progressive multiple sequence alignment method has been greatly improved for the alignment of divergent protein sequences. Firstly, individual weights are assigned to each sequence in a partial alignment in order to down-weight near-duplicate sequences and up-weight the most divergent ones. Secondly, amino acid substitution matrices are varied at different alignment stages according to the divergence of the sequences to be aligned. Thirdly, residue-specific gap penalties and locally reduced gap penalties in hydrophilic regions encourage new gaps in potential loop regions rather than regular secondary structure. Fourthly, positions in early alignments where gaps have been opened receive locally reduced gap penalties to encourage the opening up of new gaps at these positions. These modifications are incorporated into a new program, CLUSTAL W which is freely available.

63,427 citations

Journal Article•DOI•
TL;DR: A computer program that progressively evaluates the hydrophilicity and hydrophobicity of a protein along its amino acid sequence has been devised and its simplicity and its graphic nature make it a very useful tool for the evaluation of protein structures.

21,921 citations

Journal Article•DOI•
Klaus Weber1, Mary Osborn1•
TL;DR: The results show that the polyacrylamide gel electrophoresis method can be used with great confidence to determine the molecular weights of polypeptide chains for a wide variety of proteins.

19,381 citations